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

ATP-binding cassette sub-family C member 8 (Sulfonylurea receptor 1)

 ABCC8_HUMAN             Reviewed;        1581 AA.
Q09428; A6NMX8; E3UYX6; O75948; Q16583;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 6.
30-AUG-2017, entry version 185.
RecName: Full=ATP-binding cassette sub-family C member 8;
AltName: Full=Sulfonylurea receptor 1;
Name=ABCC8; Synonyms=HRINS, SUR, SUR1;
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 3).
TISSUE=Heart;
PubMed=21671119; DOI=10.1007/s00018-011-0739-x;
Schmid D., Stolzlechner M., Sorgner A., Bentele C., Assinger A.,
Chiba P., Moeslinger T.;
"An abundant, truncated human sulfonylurea receptor 1 splice variant
has prodiabetic properties and impairs sulfonylurea action.";
Cell. Mol. Life Sci. 69:129-148(2012).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND
VARIANT SER-1369.
TISSUE=Pancreatic islet;
Gonzalez G., Aguilar-Bryan L., Bryan J.;
"Human beta cell sulfonylurea receptor, SUR1, expression.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT
SER-1369, AND VARIANT PNDM PRO-225.
TISSUE=Brain, and Foreskin;
Thomas P.T., Wohllk N., Huang E., Gagel R.F., Cote G.J.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-1369.
TISSUE=Pancreas;
Nishimura M., Miki T., Aizawa T., Seino S.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1187-1581, AND VARIANT SER-1369.
TISSUE=Pancreatic islet;
PubMed=7716548; DOI=10.1126/science.7716548;
Thomas P.M., Cote G.J., Wohllk N., Haddad B., Mathew P.M., Rabl W.,
Aguilar-Bryan L., Gagel R.F., Bryan J.;
"Mutations in the sulfonylurea receptor gene in familial persistent
hyperinsulinemic hypoglycemia of infancy.";
Science 268:426-429(1995).
[7]
TOPOLOGY.
PubMed=10506167; DOI=10.1074/jbc.274.41.29122;
Raab-Graham K.F., Cirilo L.J., Boettcher A.A., Radeke C.M.,
Vandenberg C.A.;
"Membrane topology of the amino-terminal region of the sulfonylurea
receptor.";
J. Biol. Chem. 274:29122-29129(1999).
[8]
REVIEW.
PubMed=10204114; DOI=10.1210/edrv.20.2.0361;
Aguilar-Bryan L., Bryan J.;
"Molecular biology of adenosine triphosphate-sensitive potassium
channels.";
Endocr. Rev. 20:101-135(1999).
[9]
REVIEW ON VARIANTS.
PubMed=10338089;
DOI=10.1002/(SICI)1098-1004(1999)13:5<351::AID-HUMU3>3.0.CO;2-R;
Meissner T., Beinbrech B., Mayatepek E.;
"Congenital hyperinsulinism: molecular basis of a heterogeneous
disease.";
Hum. Mutat. 13:351-361(1999).
[10]
VARIANT HHF1 VAL-716.
PubMed=8751851;
Thomas P.M., Wohllk N., Huang E., Kuhnle U., Rabl W., Gagel R.F.,
Cote G.J.;
"Inactivation of the first nucleotide-binding fold of the sulfonylurea
receptor, and familial persistent hyperinsulinemic hypoglycemia of
infancy.";
Am. J. Hum. Genet. 59:510-518(1996).
[11]
VARIANT SER-1369.
PubMed=8635661; DOI=10.2337/diab.45.6.825;
Inoue H., Ferrer J., Welling C.M., Elbein S.C., Hoffman M.,
Mayorga R., Warren-Perry M., Zhang Y., Millns H., Turner R.,
Province M., Bryan J., Permutt M.A., Aguilar-Bryan L.;
"Sequence variants in the sulfonylurea receptor (SUR) gene are
associated with NIDDM in Caucasians.";
Diabetes 45:825-831(1996).
[12]
VARIANT HHF1 PHE-1387 DEL, AND VARIANTS GLY-1360; SER-1369 AND
ILE-1572.
PubMed=8923011; DOI=10.1093/hmg/5.11.1813;
Nestorowicz A., Wilson B.A., Schoor K.P., Inoue H., Glaser B.,
Landau H., Stanley C.A., Thornton P.S., Clement J.P. IV, Bryan J.,
Aguilar-Bryan L., Permutt M.A.;
"Mutations in the sulfonylurea receptor gene are associated with
familial hyperinsulinism in Ashkenazi Jews.";
Hum. Mol. Genet. 5:1813-1822(1996).
[13]
CHARACTERIZATION OF VARIANT HHF1 ARG-1478.
PubMed=8650576; DOI=10.1126/science.272.5269.1785;
Nichols C.G., Shyng S.-L., Nestorowicz A., Glaser B., Clement J.P. IV,
Gonzalez G., Aguilar-Bryan L., Permutt M.A., Bryan J.;
"Adenosine diphosphate as an intracellular regulator of insulin
secretion.";
Science 272:1785-1787(1996).
[14]
VARIANTS GLN-275; MET-560; ASN-810; CYS-834 AND SER-1369.
PubMed=9519757; DOI=10.2337/diabetes.47.3.476;
Ohta Y., Tanizawa Y., Inoue H., Hosaka T., Ueda K., Matsutani A.,
Repunte V.P., Yamada M., Kurachi Y., Bryan J., Aguilar-Bryan L.,
Permutt M.A., Oka Y.;
"Identification and functional analysis of sulfonylurea receptor 1
variants in Japanese patients with NIDDM.";
Diabetes 47:476-481(1998).
[15]
VARIANTS ASN-673 AND SER-1369.
PubMed=9568693; DOI=10.2337/diabetes.47.4.598;
Hansen T., Echwald S.M., Hansen L., Moeller A.M., Almind K.,
Clausen J.O., Urhammer S.A., Inoue H., Ferrer J., Bryan J.,
Aguilar-Bryan L., Permutt M.A., Pedersen O.;
"Decreased tolbutamide-stimulated insulin secretion in healthy
subjects with sequence variants in the high-affinity sulfonylurea
receptor gene.";
Diabetes 47:598-605(1998).
[16]
CHARACTERIZATION OF VARIANTS HHF1 GLN-125; SER-188; LEU-591; MET-1138;
GLN-1214; SER-1381; PHE-1387 DEL AND HIS-1393.
PubMed=9648840; DOI=10.2337/diabetes.47.7.1145;
Shyng S.-L., Ferrigni T., Shepard J.B., Nestorowicz A., Glaser B.,
Permutt M.A., Nichols C.G.;
"Functional analyses of novel mutations in the sulfonylurea receptor 1
associated with persistent hyperinsulinemic hypoglycemia of infancy.";
Diabetes 47:1145-1151(1998).
[17]
VARIANTS HHF1 GLN-74; GLN-125; SER-188; ASP-406; LEU-591; MET-1138;
GLN-1214; ARG-1378; SER-1381; PHE-1387 DEL AND HIS-1393.
PubMed=9618169; DOI=10.1093/hmg/7.7.1119;
Nestorowicz A., Glaser B., Wilson B.A., Shyng S.-L., Nichols C.G.,
Stanley C.A., Thornton P.S., Permutt M.A.;
"Genetic heterogeneity in familial hyperinsulinism.";
Hum. Mol. Genet. 7:1119-1128(1998).
[18]
VARIANTS HHF1 PRO-1352; CYS-1420 AND TRP-1493.
PubMed=9769320; DOI=10.1172/JCI4495;
Verkarre V., Fournet J.-C., de Lonlay P., Gross-Morand M.-S.,
Devillers M., Rahier J., Brunelle F., Robert J.-J., Nihoul-Fekete C.,
Saudubray J.-M., Junien C.;
"Paternal mutation of the sulfonylurea receptor (SUR1) gene and
maternal loss of 11p15 imprinted genes lead to persistent
hyperinsulinism in focal adenomatous hyperplasia.";
J. Clin. Invest. 102:1286-1291(1998).
[19]
VARIANT HHF1 ASP-187.
PubMed=10334322; DOI=10.2337/diabetes.48.2.408;
Otonkoski T., Aemmaelae C., Huopio H., Cote G.J., Chapman J.,
Cosgrove K., Ashfield R., Huang E., Komulainen J., Ashcroft F.M.,
Dunne M.J., Kere J., Thomas P.M.;
"A point mutation inactivating the sulfonylurea receptor causes the
severe form of persistent hyperinsulinemic hypoglycemia of infancy in
Finland.";
Diabetes 48:408-415(1999).
[20]
VARIANTS SER-1369 AND ILE-1572.
PubMed=10447255;
DOI=10.1002/(SICI)1098-1004(1999)14:1<23::AID-HUMU3>3.0.CO;2-#;
Glaser B., Furth J., Stanley C.A., Baker L., Thornton P.S., Landau H.,
Permutt M.A.;
"Intragenic single nucleotide polymorphism haplotype analysis of SUR1
mutations in familial hyperinsulinism.";
Hum. Mutat. 14:23-29(1999).
[21]
VARIANTS HHF1 GLY-841; CYS-1420 AND TRP-1493.
PubMed=10202168; DOI=10.1056/NEJM199904153401505;
de Lonlay-Debeney P., Poggi-Travert F., Fournet J.-C., Sempoux C.,
Vici C.D., Brunelle F., Touati G., Rahier J., Junien C.,
Nihoul-Fekete C., Robert J.-J., Saudubray J.-M.;
"Clinical features of 52 neonates with hyperinsulinism.";
N. Engl. J. Med. 340:1169-1175(1999).
[22]
CHARACTERIZATION OF VARIANTS HHF1 CYS-1420 AND GLN-1436, AND VARIANT
SER-1369.
PubMed=10615958; DOI=10.2337/diabetes.49.1.114;
Tanizawa Y., Matsuda K., Matsuo M., Ohta Y., Ochi N., Adachi M.,
Koga M., Mizuno S., Kajita M., Tanaka Y., Tachibana K., Inoue H.,
Furukawa S., Amachi T., Ueda K., Oka Y.;
"Genetic analysis of Japanese patients with persistent
hyperinsulinemic hypoglycemia of infancy: nucleotide-binding fold-2
mutation impairs cooperative binding of adenine nucleotides to
sulfonylurea receptor 1.";
Diabetes 49:114-120(2000).
[23]
CHARACTERIZATION OF VARIANT HHF1 LYS-1506.
PubMed=11018078; DOI=10.1172/JCI9804;
Huopio H., Reimann F., Ashfield R., Komulainen J., Lenko H.-L.,
Rahier J., Vauhkonen I., Kere J., Laakso M., Ashcroft F.,
Otonkoski T.;
"Dominantly inherited hyperinsulinism caused by a mutation in the
sulfonylurea receptor type 1.";
J. Clin. Invest. 106:897-906(2000).
[24]
CHARACTERIZATION OF VARIANT HHF1 PHE-1387 DEL.
PubMed=11226335; DOI=10.1073/pnas.051499698;
Cartier E.A., Conti L.R., Vandenberg C.A., Shyng S.-L.;
"Defective trafficking and function of KATP channels caused by a
sulfonylurea receptor 1 mutation associated with persistent
hyperinsulinemic hypoglycemia of infancy.";
Proc. Natl. Acad. Sci. U.S.A. 98:2882-2887(2001).
[25]
CHARACTERIZATION OF VARIANT HHF1 PRO-1543.
PubMed=11867634; DOI=10.1074/jbc.M200363200;
Taschenberger G., Mougey A., Shen S., Lester L.B., LaFranchi S.,
Shyng S.-L.;
"Identification of a familial hyperinsulinism-causing mutation in the
sulfonylurea receptor 1 that prevents normal trafficking and function
of KATP channels.";
J. Biol. Chem. 277:17139-17146(2002).
[26]
VARIANTS HHF1 ASP-187; THR-1457; LYS-1506; ASP-1550 AND VAL-1551.
PubMed=12364426; DOI=10.1210/jc.2002-020378;
Huopio H., Jaeaeskelaeinen J., Komulainen J., Miettinen R.,
Kaerkkaeinen P., Laakso M., Tapanainen P., Voutilainen R.,
Otonkoski T.;
"Acute insulin response tests for the differential diagnosis of
congenital hyperinsulinism.";
J. Clin. Endocrinol. Metab. 87:4502-4507(2002).
[27]
VARIANT HHF1 SER-1385 DEL, AND CHARACTERIZATION OF VARIANT HHF1
SER-1385 DEL.
PubMed=12941782; DOI=10.2337/diabetes.52.9.2403;
Thornton P.S., MacMullen C., Ganguly A., Ruchelli E., Steinkrauss L.,
Crane A., Aguilar-Bryan L., Stanley C.A.;
"Clinical and molecular characterization of a dominant form of
congenital hyperinsulinism caused by a mutation in the high-affinity
sulfonylurea receptor.";
Diabetes 52:2403-2410(2003).
[28]
VARIANT LIH HIS-1352, AND CHARACTERIZATION OF VARIANT LIH HIS-1352.
PubMed=15356046; DOI=10.1210/jc.2004-0441;
Magge S.N., Shyng S.-L., MacMullen C., Steinkrauss L., Ganguly A.,
Katz L.E.L., Stanley C.A.;
"Familial leucine-sensitive hypoglycemia of infancy due to a dominant
mutation of the beta-cell sulfonylurea receptor.";
J. Clin. Endocrinol. Metab. 89:4450-4456(2004).
[29]
VARIANTS HHF1 GLU-70; ARG-111; GLU-1342; HIS-1418 AND TRP-1493, AND
CHARACTERIZATION OF VARIANTS HHF1 GLU-70; ARG-111; GLU-1342; HIS-1418
AND TRP-1493.
PubMed=15579781; DOI=10.1210/jc.2004-1233;
Tornovsky S., Crane A., Cosgrove K.E., Hussain K., Lavie J.,
Heyman M., Nesher Y., Kuchinski N., Ben-Shushan E., Shatz O.,
Nahari E., Potikha T., Zangen D., Tenenbaum-Rakover Y., de Vries L.,
Argente J., Gracia R., Landau H., Eliakim A., Lindley K., Dunne M.J.,
Aguilar-Bryan L., Glaser B.;
"Hyperinsulinism of infancy: novel ABCC8 and KCNJ11 mutations and
evidence for additional locus heterogeneity.";
J. Clin. Endocrinol. Metab. 89:6224-6234(2004).
[30]
VARIANTS HHF1 GLN-1384 AND LYS-1486, AND VARIANT SER-1369.
PubMed=15807877; DOI=10.1111/j.1365-2265.2005.02242.x;
Ohkubo K., Nagashima M., Naito Y., Taguchi T., Suita S., Okamoto N.,
Fujinaga H., Tsumura K., Kikuchi K., Ono J.;
"Genotypes of the pancreatic beta-cell K-ATP channel and clinical
phenotypes of Japanese patients with persistent hyperinsulinaemic
hypoglycaemia of infancy.";
Clin. Endocrinol. (Oxf.) 62:458-465(2005).
[31]
VARIANTS HHF1 SER-27; TRP-74; SER-188; GLN-495; LYS-501; SER-686;
TRP-1214; GLN-1214; ASN-1336; PHE-1387 DEL; HIS-1471 AND ASN-1471.
PubMed=15562009; DOI=10.1210/jc.2004-1604;
Henwood M.J., Kelly A., MacMullen C., Bhatia P., Ganguly A.,
Thornton P.S., Stanley C.A.;
"Genotype-phenotype correlations in children with congenital
hyperinsulinism due to recessive mutations of the adenosine
triphosphate-sensitive potassium channel genes.";
J. Clin. Endocrinol. Metab. 90:789-794(2005).
[32]
VARIANT PNDM LEU-132, AND CHARACTERIZATION OF VARIANT PNDM LEU-132.
PubMed=16613899; DOI=10.1093/hmg/ddl101;
Proks P., Arnold A.L., Bruining J., Girard C., Flanagan S.E.,
Larkin B., Colclough K., Hattersley A.T., Ashcroft F.M., Ellard S.;
"A heterozygous activating mutation in the sulphonylurea receptor SUR1
(ABCC8) causes neonatal diabetes.";
Hum. Mol. Genet. 15:1793-1800(2006).
[33]
VARIANTS HHF1 TRP-74; ARG-111; SER-188; ARG-233; ASN-310; ARG-551;
THR-719; PRO-1130; ARG-1147; LYS-1295 AND PRO-1450, AND VARIANTS
SER-1369 AND ILE-1572.
PubMed=16429405; DOI=10.1002/humu.9401;
Fernandez-Marmiesse A., Salas A., Vega A., Fernandez-Lorenzo J.R.,
Barreiro J., Carracedo A.;
"Mutation spectra of ABCC8 gene in Spanish patients with
Hyperinsulinism of Infancy (HI).";
Hum. Mutat. 27:214-214(2006).
[34]
VARIANTS HHF1 ARG-7; ASP-21; SER-27; TRP-74; LYS-501; PRO-503;
SER-686; TRP-1214; TRP-1214; GLN-1349; ARG-1378; PHE-1387 DEL;
ARG-1400 AND GLN-1493.
PubMed=16357843; DOI=10.1038/modpathol.3800497;
Suchi M., MacMullen C.M., Thornton P.S., Adzick N.S., Ganguly A.,
Ruchelli E.D., Stanley C.A.;
"Molecular and immunohistochemical analyses of the focal form of
congenital hyperinsulinism.";
Mod. Pathol. 19:122-129(2006).
[35]
VARIANTS PNDM ARG-213 AND VAL-1424, VARIANTS TNDM2 ARG-435; VAL-582;
TYR-1023; GLN-1182 AND CYS-1379, CHARACTERIZATION OF VARIANT PNDM
VAL-1424, AND CHARACTERIZATION OF VARIANT TNDM2 TYR-1023.
PubMed=16885549; DOI=10.1056/NEJMoa055068;
Babenko A.P., Polak M., Cave H., Busiah K., Czernichow P.,
Scharfmann R., Bryan J., Aguilar-Bryan L., Vaxillaire M., Froguel P.;
"Activating mutations in the ABCC8 gene in neonatal diabetes
mellitus.";
N. Engl. J. Med. 355:456-466(2006).
[36]
VARIANTS PNDM LEU-45; SER-72; ALA-86; GLY-86; LEU-132; VAL-132;
SER-207; LYS-208; GLU-209; LYS-211; PRO-225; ILE-229; ASP-263;
LYS-382; GLU-1184; LYS-1326; ARG-1400 AND LEU-1522, AND
CHARACTERIZATION OF VARIANTS PNDM LEU-132; SER-207; ILE-229; GLU-1184
AND LEU-1522.
PubMed=17668386; DOI=10.1086/519174;
Ellard S., Flanagan S.E., Girard C.A., Patch A.M., Harries L.W.,
Parrish A., Edghill E.L., Mackay D.J., Proks P., Shimomura K.,
Haberland H., Carson D.J., Shield J.P., Hattersley A.T.,
Ashcroft F.M.;
"Permanent neonatal diabetes caused by dominant, recessive, or
compound heterozygous SUR1 mutations with opposite functional
effects.";
Am. J. Hum. Genet. 81:375-382(2007).
[37]
VARIANT PNDM ALA-86.
PubMed=17213273; DOI=10.1210/jc.2006-2490;
Stanik J., Gasperikova D., Paskova M., Barak L., Javorkova J.,
Jancova E., Ciljakova M., Hlava P., Michalek J., Flanagan S.E.,
Pearson E., Hattersley A.T., Ellard S., Klimes I.;
"Prevalence of permanent neonatal diabetes in Slovakia and successful
replacement of insulin with sulfonylurea therapy in KCNJ11 and ABCC8
mutation carriers.";
J. Clin. Endocrinol. Metab. 92:1276-1282(2007).
[38]
VARIANTS HHF1 MET-511; ASP-716; LYS-824; THR-889; PRO-890; PRO-1352;
SER-1378; PHE-1386; TYR-1388; PRO-1389; VAL-1457; ILE-1480; GLU-1505
AND SER-1511, CHARACTERIZATION OF VARIANTS HHF1 MET-511; LYS-824;
THR-889; PRO-890; SER-1378; VAL-1457; ILE-1480; GLU-1505 AND SER-1511,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24814349; DOI=10.1111/cge.12428;
Saint-Martin C., Zhou Q., Martin G.M., Vaury C., Leroy G.,
Arnoux J.B., de Lonlay P., Shyng S.L., Bellanne-Chantelot C.;
"Monoallelic ABCC8 mutations are a common cause of diazoxide-
unresponsive diffuse form of congenital hyperinsulinism.";
Clin. Genet. 87:448-454(2015).
[39]
VARIANT HHF1 HIS-1418, CHARACTERIZATION OF VARIANT HHF1 HIS-1418, AND
FUNCTION.
PubMed=25720052; DOI=10.1515/jpem-2014-0265;
Harel S., Cohen A.S., Hussain K., Flanagan S.E., Schlade-Bartusiak K.,
Patel M., Courtade J., Li J.B., Van Karnebeek C., Kurata H.,
Ellard S., Chanoine J.P., Gibson W.T.;
"Alternating hypoglycemia and hyperglycemia in a toddler with a
homozygous p.R1419H ABCC8 mutation: an unusual clinical picture.";
J. Pediatr. Endocrinol. Metab. 28:345-351(2015).
-!- FUNCTION: Subunit of the beta-cell ATP-sensitive potassium channel
(KATP). Regulator of ATP-sensitive K(+) channels and insulin
release. {ECO:0000269|PubMed:24814349,
ECO:0000269|PubMed:25720052}.
-!- SUBUNIT: Interacts with KCNJ11.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24814349};
Multi-pass membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q09428-1; Sequence=Displayed;
Name=2;
IsoId=Q09428-2; Sequence=VSP_000055;
Name=3; Synonyms=SUR1Delta2;
IsoId=Q09428-3; Sequence=VSP_044090;
Note=Abundant isoform with prodiabetic properties, predominant
in heart.;
-!- DISEASE: Leucine-induced hypoglycemia (LIH) [MIM:240800]: Rare
cause of hypoglycemia and is described as a condition in which
symptomatic hypoglycemia is provoked by high protein feedings.
Hypoglycemia is also elicited by administration of oral or
intravenous infusions of a single amino acid, leucine.
{ECO:0000269|PubMed:15356046}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Familial hyperinsulinemic hypoglycemia 1 (HHF1)
[MIM:256450]: Most common cause of persistent hypoglycemia in
infancy. Unless early and aggressive intervention is undertaken,
brain damage from recurrent episodes of hypoglycemia may occur.
{ECO:0000269|PubMed:10202168, ECO:0000269|PubMed:10334322,
ECO:0000269|PubMed:10615958, ECO:0000269|PubMed:11018078,
ECO:0000269|PubMed:11226335, ECO:0000269|PubMed:11867634,
ECO:0000269|PubMed:12364426, ECO:0000269|PubMed:12941782,
ECO:0000269|PubMed:15562009, ECO:0000269|PubMed:15579781,
ECO:0000269|PubMed:15807877, ECO:0000269|PubMed:16357843,
ECO:0000269|PubMed:16429405, ECO:0000269|PubMed:24814349,
ECO:0000269|PubMed:25720052, ECO:0000269|PubMed:8650576,
ECO:0000269|PubMed:8751851, ECO:0000269|PubMed:8923011,
ECO:0000269|PubMed:9618169, ECO:0000269|PubMed:9648840,
ECO:0000269|PubMed:9769320}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Diabetes mellitus, permanent neonatal (PNDM)
[MIM:606176]: A rare form of diabetes distinct from childhood-
onset autoimmune diabetes mellitus type 1. It is characterized by
insulin-requiring hyperglycemia that is diagnosed within the first
months of life. Permanent neonatal diabetes requires lifelong
therapy. {ECO:0000269|PubMed:16613899,
ECO:0000269|PubMed:16885549, ECO:0000269|PubMed:17213273,
ECO:0000269|PubMed:17668386}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Transient neonatal diabetes mellitus 2 (TNDM2)
[MIM:610374]: Neonatal diabetes is a form of diabetes mellitus
defined by the onset of mild-to-severe hyperglycemia within the
first months of life. Transient neonatal diabetes remits early,
with a possible relapse during adolescence.
{ECO:0000269|PubMed:16885549}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q09428";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; HM635782; ADM67556.1; -; mRNA.
EMBL; L78207; AAB02278.1; -; mRNA.
EMBL; L78243; AAB02417.1; -; Genomic_DNA.
EMBL; L78208; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78209; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78210; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78211; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78212; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78255; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78213; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78214; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78215; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78216; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78217; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78218; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78219; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78220; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78221; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78222; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78223; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78225; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78254; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78226; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78227; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78228; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78229; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78230; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78231; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78232; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78233; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78234; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78235; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78236; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78237; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78238; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78239; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78240; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78241; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78242; AAB02417.1; JOINED; Genomic_DNA.
EMBL; L78243; AAB02418.1; -; Genomic_DNA.
EMBL; L78208; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78209; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78210; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78211; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78212; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78255; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78213; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78214; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78215; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78216; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78217; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78218; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78219; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78220; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78221; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78222; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78224; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78225; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78254; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78226; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78227; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78228; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78229; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78230; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78231; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78232; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78233; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78234; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78235; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78236; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78237; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78238; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78239; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78240; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78241; AAB02418.1; JOINED; Genomic_DNA.
EMBL; L78242; AAB02418.1; JOINED; Genomic_DNA.
EMBL; U63421; AAB36699.1; -; mRNA.
EMBL; U63455; AAB36700.1; -; Genomic_DNA.
EMBL; U63422; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63423; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63424; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63425; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63426; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63427; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63428; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63429; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63430; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63431; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63432; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63433; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63434; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63435; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63436; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63437; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63438; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63439; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63441; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63442; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63443; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63444; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63445; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63446; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63447; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63448; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63449; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63450; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63451; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63452; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63453; AAB36700.1; JOINED; Genomic_DNA.
EMBL; U63454; AAB36700.1; JOINED; Genomic_DNA.
EMBL; AF087138; AAC36724.1; -; mRNA.
EMBL; AC124798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L40625; AAA99227.1; -; mRNA.
CCDS; CCDS31437.1; -. [Q09428-1]
CCDS; CCDS73264.1; -. [Q09428-2]
RefSeq; NP_000343.2; NM_000352.4. [Q09428-1]
RefSeq; NP_001274103.1; NM_001287174.1. [Q09428-2]
UniGene; Hs.54470; -.
ProteinModelPortal; Q09428; -.
BioGrid; 112700; 2.
DIP; DIP-58642N; -.
ELM; Q09428; -.
STRING; 9606.ENSP00000374467; -.
BindingDB; Q09428; -.
ChEMBL; CHEMBL2071; -.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB00672; Chlorpropamide.
DrugBank; DB01120; Gliclazide.
DrugBank; DB00222; Glimepiride.
DrugBank; DB01067; Glipizide.
DrugBank; DB01251; Gliquidone.
DrugBank; DB01016; Glyburide.
DrugBank; DB01382; Glycodiazine.
DrugBank; DB01252; Mitiglinide.
DrugBank; DB00731; Nateglinide.
DrugBank; DB00912; Repaglinide.
DrugBank; DB00839; Tolazamide.
DrugBank; DB01124; Tolbutamide.
GuidetoPHARMACOLOGY; 2594; -.
TCDB; 3.A.1.208.4; the atp-binding cassette (abc) superfamily.
iPTMnet; Q09428; -.
PhosphoSitePlus; Q09428; -.
BioMuta; ABCC8; -.
DMDM; 311033501; -.
EPD; Q09428; -.
PaxDb; Q09428; -.
PeptideAtlas; Q09428; -.
PRIDE; Q09428; -.
DNASU; 6833; -.
Ensembl; ENST00000302539; ENSP00000303960; ENSG00000006071. [Q09428-2]
Ensembl; ENST00000389817; ENSP00000374467; ENSG00000006071. [Q09428-1]
Ensembl; ENST00000612903; ENSP00000483031; ENSG00000006071. [Q09428-3]
GeneID; 6833; -.
KEGG; hsa:6833; -.
UCSC; uc001mnc.4; human. [Q09428-1]
CTD; 6833; -.
DisGeNET; 6833; -.
GeneCards; ABCC8; -.
GeneReviews; ABCC8; -.
H-InvDB; HIX0035864; -.
HGNC; HGNC:59; ABCC8.
HPA; CAB011451; -.
HPA; HPA042318; -.
MalaCards; ABCC8; -.
MIM; 240800; phenotype.
MIM; 256450; phenotype.
MIM; 600509; gene.
MIM; 602485; phenotype.
MIM; 606176; phenotype.
MIM; 610374; phenotype.
neXtProt; NX_Q09428; -.
OpenTargets; ENSG00000006071; -.
Orphanet; 276575; Autosomal dominant hyperinsulinism due to SUR1 deficiency.
Orphanet; 79643; Autosomal recessive hyperinsulinism due to SUR1 deficiency.
Orphanet; 79134; DEND syndrome.
Orphanet; 276598; Diazoxide-resistant focal hyperinsulinism due to SUR1 deficiency.
Orphanet; 552; MODY.
Orphanet; 99885; Permanent neonatal diabetes mellitus.
Orphanet; 99886; Transient neonatal diabetes mellitus.
PharmGKB; PA24395; -.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00880000137856; -.
HOVERGEN; HBG101342; -.
InParanoid; Q09428; -.
KO; K05032; -.
OMA; MEYIGAC; -.
OrthoDB; EOG091G00IN; -.
PhylomeDB; Q09428; -.
TreeFam; TF105201; -.
Reactome; R-HSA-1296025; ATP sensitive Potassium channels.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-5683177; Defective ABCC8 can cause hypoglycemias and hyperglycemias.
SignaLink; Q09428; -.
ChiTaRS; ABCC8; human.
GeneWiki; ABCC8; -.
GenomeRNAi; 6833; -.
PRO; PR:Q09428; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000006071; -.
CleanEx; HS_ABCC8; -.
ExpressionAtlas; Q09428; baseline and differential.
Genevisible; Q09428; HS.
GO; GO:0008282; C:ATP-sensitive potassium channel complex; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; TAS:Reactome.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0043225; F:ATPase-coupled anion transmembrane transporter activity; TAS:Reactome.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0005267; F:potassium channel activity; IMP:UniProtKB.
GO; GO:0008281; F:sulfonylurea receptor activity; IEA:InterPro.
GO; GO:0019905; F:syntaxin binding; IEA:Ensembl.
GO; GO:0001678; P:cellular glucose homeostasis; IEA:Ensembl.
GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:1905604; P:negative regulation of maintenance of permeability of blood-brain barrier; IEA:Ensembl.
GO; GO:0061855; P:negative regulation of neuroblast migration; IEA:Ensembl.
GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
GO; GO:1905075; P:positive regulation of occluding junction disassembly; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:1900721; P:positive regulation of uterine smooth muscle relaxation; IEA:Ensembl.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:Ensembl.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0042493; P:response to drug; IBA:GO_Central.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009268; P:response to pH; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR000844; ABCC8.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000388; Sulphorea_rcpt.
PANTHER; PTHR24223:SF293; PTHR24223:SF293; 1.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
PRINTS; PR01093; SULFNYLUR1.
PRINTS; PR01092; SULFNYLUREAR.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Diabetes mellitus; Disease mutation; Glycoprotein; Membrane;
Nucleotide-binding; Polymorphism; Receptor; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1581 ATP-binding cassette sub-family C member
8.
/FTId=PRO_0000093400.
TOPO_DOM 1 34 Extracellular. {ECO:0000250}.
TRANSMEM 35 55 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 56 75 Cytoplasmic. {ECO:0000250}.
TRANSMEM 76 96 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 97 101 Extracellular. {ECO:0000250}.
TRANSMEM 102 122 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 123 134 Cytoplasmic. {ECO:0000250}.
TRANSMEM 135 154 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 155 167 Extracellular. {ECO:0000250}.
TRANSMEM 168 194 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 195 311 Cytoplasmic. {ECO:0000250}.
TRANSMEM 312 331 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 332 355 Extracellular. {ECO:0000250}.
TRANSMEM 356 376 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 377 434 Cytoplasmic. {ECO:0000250}.
TRANSMEM 435 455 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 456 458 Extracellular. {ECO:0000250}.
TRANSMEM 459 479 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 480 541 Cytoplasmic. {ECO:0000250}.
TRANSMEM 542 562 Helical; Name=10. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 563 584 Extracellular. {ECO:0000250}.
TRANSMEM 585 605 Helical; Name=11. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 606 1004 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1005 1025 Helical; Name=12. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1026 1072 Extracellular. {ECO:0000250}.
TRANSMEM 1073 1093 Helical; Name=13. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1094 1137 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1138 1158 Helical; Name=14. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1159 1159 Extracellular. {ECO:0000250}.
TRANSMEM 1160 1180 Helical; Name=15. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1181 1251 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1252 1272 Helical; Name=16. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1273 1276 Extracellular. {ECO:0000250}.
TRANSMEM 1277 1297 Helical; Name=17. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1298 1581 Cytoplasmic. {ECO:0000250}.
DOMAIN 299 602 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 679 929 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1012 1306 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1344 1578 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 713 720 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1378 1385 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 10 10 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 1049 1049 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
VAR_SEQ 51 1581 Missing (in isoform 3).
{ECO:0000303|PubMed:21671119}.
/FTId=VSP_044090.
VAR_SEQ 740 740 S -> SS (in isoform 2). {ECO:0000305}.
/FTId=VSP_000055.
VARIANT 7 7 G -> R (in HHF1).
{ECO:0000269|PubMed:16357843}.
/FTId=VAR_031349.
VARIANT 21 21 V -> D (in HHF1; dbSNP:rs200670692).
{ECO:0000269|PubMed:16357843}.
/FTId=VAR_031350.
VARIANT 27 27 F -> S (in HHF1).
{ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:16357843}.
/FTId=VAR_031351.
VARIANT 45 45 P -> L (in PNDM; compound heterozygous
with R-1400; dbSNP:rs267606623).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072928.
VARIANT 70 70 G -> E (in HHF1; altered intracellular
trafficking).
{ECO:0000269|PubMed:15579781}.
/FTId=VAR_031352.
VARIANT 72 72 N -> S (in PNDM; mosaic;
dbSNP:rs80356634).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072929.
VARIANT 74 74 R -> Q (in HHF1; dbSNP:rs72559734).
{ECO:0000269|PubMed:9618169}.
/FTId=VAR_008639.
VARIANT 74 74 R -> W (in HHF1; dbSNP:rs201682634).
{ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:16357843,
ECO:0000269|PubMed:16429405}.
/FTId=VAR_031353.
VARIANT 86 86 V -> A (in PNDM; dbSNP:rs193929360).
{ECO:0000269|PubMed:17213273,
ECO:0000269|PubMed:17668386}.
/FTId=VAR_031354.
VARIANT 86 86 V -> G (in PNDM; dbSNP:rs193929360).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072930.
VARIANT 104 104 L -> V (in dbSNP:rs10400391).
/FTId=VAR_029777.
VARIANT 111 111 G -> R (in HHF1; altered intracellular
trafficking; dbSNP:rs761749884).
{ECO:0000269|PubMed:15579781,
ECO:0000269|PubMed:16429405}.
/FTId=VAR_031355.
VARIANT 116 116 A -> P (in HHF1; dbSNP:rs72559731).
/FTId=VAR_031356.
VARIANT 125 125 H -> Q (in HHF1; mild; dbSNP:rs60637558).
{ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008640.
VARIANT 132 132 F -> L (in PNDM; with neurologic
features; reduces the sensitivity of the
K(ATP) channel to inhibition by MgATP;
increases whole-cell K(ATP) current;
dbSNP:rs80356637).
{ECO:0000269|PubMed:16613899,
ECO:0000269|PubMed:17668386}.
/FTId=VAR_029778.
VARIANT 132 132 F -> V (in PNDM; dbSNP:rs80356637).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072931.
VARIANT 187 187 V -> D (in HHF1; severe; high prevalence
in Finland; loss of channel activity;
dbSNP:rs137852672).
{ECO:0000269|PubMed:10334322,
ECO:0000269|PubMed:12364426}.
/FTId=VAR_008641.
VARIANT 188 188 N -> S (in HHF1; severe;
dbSNP:rs797045213).
{ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:16429405,
ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008642.
VARIANT 207 207 P -> S (in PNDM; reduced inhibition by
ATP). {ECO:0000269|PubMed:17668386}.
/FTId=VAR_072932.
VARIANT 208 208 E -> K (in PNDM; compound heterozygous
with D-263).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072933.
VARIANT 209 209 D -> E (in PNDM; dbSNP:rs80356640).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072934.
VARIANT 211 211 Q -> K (in PNDM; dbSNP:rs193929366).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072935.
VARIANT 213 213 L -> R (in PNDM; dbSNP:rs80356642).
{ECO:0000269|PubMed:16885549}.
/FTId=VAR_029779.
VARIANT 225 225 L -> P (in PNDM; dbSNP:rs1048095).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072936.
VARIANT 229 229 T -> I (in PNDM; compound heterozygous
with L-1523; highly reduced inhibition by
ATP when associated with L-1523;
dbSNP:rs768017509).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072937.
VARIANT 233 233 M -> R (in HHF1).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031357.
VARIANT 263 263 Y -> D (in PNDM; compound heterozygous
with K-208; dbSNP:rs778892038).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072938.
VARIANT 275 275 R -> Q (in dbSNP:rs185040406).
{ECO:0000269|PubMed:9519757}.
/FTId=VAR_008643.
VARIANT 310 310 D -> N (in HHF1; dbSNP:rs769569410).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031358.
VARIANT 382 382 E -> K (in PNDM; dbSNP:rs80356651).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072939.
VARIANT 406 406 N -> D (in HHF1; dbSNP:rs72559728).
{ECO:0000269|PubMed:9618169}.
/FTId=VAR_008644.
VARIANT 418 418 C -> R (in HHF1; dbSNP:rs67254669).
/FTId=VAR_031359.
VARIANT 435 435 C -> R (in TNDM2).
{ECO:0000269|PubMed:16885549}.
/FTId=VAR_029780.
VARIANT 495 495 R -> Q (in HHF1).
{ECO:0000269|PubMed:15562009}.
/FTId=VAR_031360.
VARIANT 501 501 E -> K (in HHF1; dbSNP:rs372307320).
{ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:16357843}.
/FTId=VAR_031361.
VARIANT 503 503 L -> P (in HHF1).
{ECO:0000269|PubMed:16357843}.
/FTId=VAR_031362.
VARIANT 508 508 L -> P (in HHF1; dbSNP:rs72559727).
/FTId=VAR_031363.
VARIANT 511 511 L -> M (in HHF1; no effect on cell
membrane expression; no effect on traffic
efficiency; dramatically reduced
potassium channel response to activators
such as MgADP or to diazoxide).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072940.
VARIANT 551 551 P -> R (in HHF1).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031364.
VARIANT 560 560 V -> M (in dbSNP:rs4148619).
{ECO:0000269|PubMed:9519757}.
/FTId=VAR_008645.
VARIANT 582 582 L -> V (in TNDM2; dbSNP:rs137852674).
{ECO:0000269|PubMed:16885549}.
/FTId=VAR_029781.
VARIANT 591 591 F -> L (in HHF1; dbSNP:rs72559726).
{ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008646.
VARIANT 620 620 R -> C (in HHF1; dbSNP:rs58241708).
/FTId=VAR_031365.
VARIANT 673 673 D -> N (in dbSNP:rs777986828).
{ECO:0000269|PubMed:9568693}.
/FTId=VAR_015006.
VARIANT 686 686 F -> S (in HHF1).
{ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:16357843}.
/FTId=VAR_031366.
VARIANT 716 716 G -> D (in HHF1).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072941.
VARIANT 716 716 G -> V (in HHF1; dbSNP:rs72559723).
{ECO:0000269|PubMed:8751851}.
/FTId=VAR_000100.
VARIANT 719 719 K -> T (in HHF1).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031367.
VARIANT 810 810 D -> N (in dbSNP:rs767572066).
{ECO:0000269|PubMed:9519757}.
/FTId=VAR_008647.
VARIANT 824 824 E -> K (in HHF1; no effect on cell
membrane expression; no effect on traffic
efficiency; dramatically reduced
potassium channel response to activators
such as MgADP or to diazoxide).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072942.
VARIANT 834 834 R -> C (in dbSNP:rs140068774).
{ECO:0000269|PubMed:9519757}.
/FTId=VAR_008648.
VARIANT 841 841 R -> G (in HHF1).
{ECO:0000269|PubMed:10202168}.
/FTId=VAR_031368.
VARIANT 889 889 K -> T (in HHF1; no effect on cell
membrane expression; no effect on traffic
efficiency; reduced potassium channel
response to activators such as MgADP or
to diazoxide; dbSNP:rs761862121).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_031369.
VARIANT 890 890 L -> P (in HHF1; no effect on cell
membrane expression; no effect on traffic
efficiency; dramatically reduced
potassium channel response to activators
such as MgADP or to diazoxide).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072943.
VARIANT 956 956 S -> F (in HHF1; dbSNP:rs72559721).
/FTId=VAR_031370.
VARIANT 1023 1023 H -> Y (in TNDM2; overactive channel).
{ECO:0000269|PubMed:16885549}.
/FTId=VAR_029782.
VARIANT 1130 1130 T -> P (in HHF1).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031371.
VARIANT 1138 1138 T -> M (in HHF1; dbSNP:rs201351976).
{ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008649.
VARIANT 1147 1147 L -> R (in HHF1).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031372.
VARIANT 1182 1182 R -> Q (in TNDM2; dbSNP:rs193922400).
{ECO:0000269|PubMed:16885549}.
/FTId=VAR_029783.
VARIANT 1184 1184 A -> E (in PNDM; slightly reduced
inhibition by ATP; dbSNP:rs137852675).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072944.
VARIANT 1214 1214 R -> Q (in HHF1; severe;
dbSNP:rs367850779).
{ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008650.
VARIANT 1214 1214 R -> W (in HHF1; dbSNP:rs139964066).
{ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:16357843}.
/FTId=VAR_031373.
VARIANT 1295 1295 N -> K (in HHF1).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031374.
VARIANT 1326 1326 E -> K (in PNDM; dbSNP:rs200563930).
{ECO:0000269|PubMed:17668386}.
/FTId=VAR_072945.
VARIANT 1336 1336 K -> N (in HHF1; dbSNP:rs67767715).
{ECO:0000269|PubMed:15562009}.
/FTId=VAR_031375.
VARIANT 1342 1342 G -> E (in HHF1; altered intracellular
trafficking).
{ECO:0000269|PubMed:15579781}.
/FTId=VAR_031376.
VARIANT 1349 1349 L -> Q (in HHF1).
{ECO:0000269|PubMed:16357843}.
/FTId=VAR_031377.
VARIANT 1352 1352 R -> H (in LIH; partially impairs ATP-
dependent potassium channel function;
dbSNP:rs28936370).
{ECO:0000269|PubMed:15356046}.
/FTId=VAR_029784.
VARIANT 1352 1352 R -> P (in HHF1; dbSNP:rs28936370).
{ECO:0000269|PubMed:24814349,
ECO:0000269|PubMed:9769320}.
/FTId=VAR_008537.
VARIANT 1360 1360 V -> G. {ECO:0000269|PubMed:8923011}.
/FTId=VAR_008651.
VARIANT 1360 1360 V -> M (in HHF1).
/FTId=VAR_015007.
VARIANT 1369 1369 A -> S (in dbSNP:rs757110).
{ECO:0000269|PubMed:10447255,
ECO:0000269|PubMed:10615958,
ECO:0000269|PubMed:15807877,
ECO:0000269|PubMed:16429405,
ECO:0000269|PubMed:7716548,
ECO:0000269|PubMed:8635661,
ECO:0000269|PubMed:8923011,
ECO:0000269|PubMed:9519757,
ECO:0000269|PubMed:9568693,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.4}.
/FTId=VAR_008652.
VARIANT 1378 1378 G -> R (in HHF1).
{ECO:0000269|PubMed:16357843,
ECO:0000269|PubMed:9618169}.
/FTId=VAR_008653.
VARIANT 1378 1378 G -> S (in HHF1; highly decreases cell
membrane expression; highly reduced
traffic efficiency; dramatically reduced
potassium channel response to activators
such as MgADP or to diazoxide).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072946.
VARIANT 1379 1379 R -> C (in TNDM2; dbSNP:rs137852673).
{ECO:0000269|PubMed:16885549}.
/FTId=VAR_029785.
VARIANT 1381 1381 G -> S (in HHF1; dbSNP:rs773448052).
{ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008654.
VARIANT 1384 1384 K -> Q (in HHF1).
{ECO:0000269|PubMed:15807877}.
/FTId=VAR_031378.
VARIANT 1385 1385 Missing (in HHF1; does not alter surface
expression but channels are not
functional).
{ECO:0000269|PubMed:12941782}.
/FTId=VAR_029786.
VARIANT 1386 1386 S -> F (in HHF1; dbSNP:rs72559718).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_031379.
VARIANT 1387 1387 Missing (in HHF1; severe; high frequency
in Ashkenazi Jewish patients; defective
trafficking and lack of surface
expression).
{ECO:0000269|PubMed:11226335,
ECO:0000269|PubMed:15562009,
ECO:0000269|PubMed:16357843,
ECO:0000269|PubMed:8923011,
ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008538.
VARIANT 1388 1388 S -> Y (in HHF1).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072947.
VARIANT 1389 1389 L -> P (in HHF1).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072948.
VARIANT 1393 1393 R -> H (in HHF1; severe; loss of channel
activity; dbSNP:rs769279368).
{ECO:0000269|PubMed:9618169,
ECO:0000269|PubMed:9648840}.
/FTId=VAR_008655.
VARIANT 1400 1400 G -> R (in HHF1 and PNDM; compound
heterozygous with L-45 in PNDM;
dbSNP:rs137852676).
{ECO:0000269|PubMed:16357843,
ECO:0000269|PubMed:17668386}.
/FTId=VAR_031380.
VARIANT 1418 1418 R -> H (in HHF1; altered intracellular
trafficking).
{ECO:0000269|PubMed:15579781,
ECO:0000269|PubMed:25720052}.
/FTId=VAR_031381.
VARIANT 1420 1420 R -> C (in HHF1; modest impairment of
channel function; dbSNP:rs28938469).
{ECO:0000269|PubMed:10202168,
ECO:0000269|PubMed:10615958,
ECO:0000269|PubMed:9769320}.
/FTId=VAR_008539.
VARIANT 1424 1424 I -> V (in PNDM; overactive channel;
dbSNP:rs80356653).
{ECO:0000269|PubMed:16885549}.
/FTId=VAR_029787.
VARIANT 1436 1436 R -> Q (in HHF1; cannot form a functional
channel, due to protein instability or
defective transport to the membrane;
dbSNP:rs387906407).
{ECO:0000269|PubMed:10615958}.
/FTId=VAR_015008.
VARIANT 1450 1450 L -> P (in HHF1).
{ECO:0000269|PubMed:16429405}.
/FTId=VAR_031382.
VARIANT 1457 1457 A -> T (in HHF1; dbSNP:rs72559717).
{ECO:0000269|PubMed:12364426}.
/FTId=VAR_031383.
VARIANT 1457 1457 A -> V (in HHF1).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072949.
VARIANT 1471 1471 D -> H (in HHF1).
{ECO:0000269|PubMed:15562009}.
/FTId=VAR_031384.
VARIANT 1471 1471 D -> N (in HHF1; dbSNP:rs72559716).
{ECO:0000269|PubMed:15562009}.
/FTId=VAR_031385.
VARIANT 1478 1478 G -> R (in HHF1; channels insensitive to
metabolic inhibition and to activation by
ADP; dbSNP:rs72559715).
{ECO:0000269|PubMed:8650576}.
/FTId=VAR_008656.
VARIANT 1480 1480 N -> I (in HHF1; no effect on cell
membrane expression; no effect on traffic
efficiency; dramatically reduced
potassium channel response to activators
such as MgADP or to diazoxide).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072950.
VARIANT 1486 1486 R -> K (in HHF1).
{ECO:0000269|PubMed:15807877}.
/FTId=VAR_031386.
VARIANT 1493 1493 R -> Q (in HHF1).
{ECO:0000269|PubMed:16357843}.
/FTId=VAR_031387.
VARIANT 1493 1493 R -> W (in HHF1; altered intracellular
trafficking; dbSNP:rs28936371).
{ECO:0000269|PubMed:10202168,
ECO:0000269|PubMed:15579781,
ECO:0000269|PubMed:9769320}.
/FTId=VAR_008540.
VARIANT 1505 1505 D -> E (in HHF1; no effect on cell
membrane expression; no effect on traffic
efficiency; dramatically reduced
potassium channel response to activators
such as MgADP or to diazoxide).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072951.
VARIANT 1506 1506 E -> K (in HHF1; mild; dominantly
inherited; channels insensitive to
metabolic inhibition and to activation by
ADP; dbSNP:rs137852671).
{ECO:0000269|PubMed:11018078,
ECO:0000269|PubMed:12364426}.
/FTId=VAR_015009.
VARIANT 1507 1507 A -> AAS (in HHF1).
/FTId=VAR_008657.
VARIANT 1511 1511 I -> S (in HHF1; no effect on cell
membrane expression; no effect on traffic
efficiency; dramatically reduced
potassium channel response to activators
such as MgADP or to diazoxide).
{ECO:0000269|PubMed:24814349}.
/FTId=VAR_072952.
VARIANT 1522 1522 V -> L (in PNDM; highly reduced
inhibition by ATP when associated whith
I-229). {ECO:0000269|PubMed:17668386}.
/FTId=VAR_072953.
VARIANT 1543 1543 L -> P (in HHF1; reduced channels surface
expression and response to ADP;
dbSNP:rs72559713).
{ECO:0000269|PubMed:11867634}.
/FTId=VAR_015010.
VARIANT 1550 1550 V -> D (in HHF1).
{ECO:0000269|PubMed:12364426}.
/FTId=VAR_031388.
VARIANT 1551 1551 L -> V (in HHF1).
{ECO:0000269|PubMed:12364426}.
/FTId=VAR_031389.
VARIANT 1572 1572 V -> I (in dbSNP:rs8192690).
{ECO:0000269|PubMed:10447255,
ECO:0000269|PubMed:16429405,
ECO:0000269|PubMed:8923011}.
/FTId=VAR_008658.
CONFLICT 30 30 A -> V (in Ref. 2; AAB02278/AAB02417/
AAB02418). {ECO:0000305}.
CONFLICT 157 157 F -> L (in Ref. 3; AAB36699/AAB36700).
{ECO:0000305}.
CONFLICT 163 163 G -> A (in Ref. 2; AAB02278/AAB02417/
AAB02418). {ECO:0000305}.
CONFLICT 167 167 L -> V (in Ref. 2; AAB02278/AAB02417/
AAB02418). {ECO:0000305}.
CONFLICT 256 256 A -> V (in Ref. 3; AAB36699/AAB36700).
{ECO:0000305}.
CONFLICT 487 487 S -> T (in Ref. 2; AAB02278/AAB02417/
AAB02418). {ECO:0000305}.
CONFLICT 1069 1070 VL -> AV (in Ref. 2; AAB02278/AAB02417/
AAB02418). {ECO:0000305}.
CONFLICT 1172 1172 I -> V (in Ref. 3; AAB36699/AAB36700).
{ECO:0000305}.
CONFLICT 1410 1410 A -> R (in Ref. 3; AAB36699/AAB36700).
{ECO:0000305}.
CONFLICT 1418 1418 R -> P (in Ref. 3; AAB36699/AAB36700).
{ECO:0000305}.
SEQUENCE 1581 AA; 176992 MW; 09CF2EC97899D1CE CRC64;
MPLAFCGSEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI
HHSTWLHFPG HNLRWILTFM LLFVLVCEIA EGILSDGVTE SHHLHLYMPA GMAFMAAVTS
VVYYHNIETS NFPKLLIALL VYWTLAFITK TIKFVKFLDH AIGFSQLRFC LTGLLVILYG
MLLLVEVNVI RVRRYIFFKT PREVKPPEDL QDLGVRFLQP FVNLLSKGTY WWMNAFIKTA
HKKPIDLRAI GKLPIAMRAL TNYQRLCEAF DAQVRKDIQG TQGARAIWQA LSHAFGRRLV
LSSTFRILAD LLGFAGPLCI FGIVDHLGKE NDVFQPKTQF LGVYFVSSQE FLANAYVLAV
LLFLALLLQR TFLQASYYVA IETGINLRGA IQTKIYNKIM HLSTSNLSMG EMTAGQICNL
VAIDTNQLMW FFFLCPNLWA MPVQIIVGVI LLYYILGVSA LIGAAVIILL APVQYFVATK
LSQAQRSTLE YSNERLKQTN EMLRGIKLLK LYAWENIFRT RVETTRRKEM TSLRAFAIYT
SISIFMNTAI PIAAVLITFV GHVSFFKEAD FSPSVAFASL SLFHILVTPL FLLSSVVRST
VKALVSVQKL SEFLSSAEIR EEQCAPHEPT PQGPASKYQA VPLRVVNRKR PAREDCRGLT
GPLQSLVPSA DGDADNCCVQ IMGGYFTWTP DGIPTLSNIT IRIPRGQLTM IVGQVGCGKS
SLLLAALGEM QKVSGAVFWS SLPDSEIGED PSPERETATD LDIRKRGPVA YASQKPWLLN
ATVEENIIFE SPFNKQRYKM VIEACSLQPD IDILPHGDQT QIGERGINLS GGQRQRISVA
RALYQHANVV FLDDPFSALD IHLSDHLMQA GILELLRDDK RTVVLVTHKL QYLPHADWII
AMKDGTIQRE GTLKDFQRSE CQLFEHWKTL MNRQDQELEK ETVTERKATE PPQGLSRAMS
SRDGLLQDEE EEEEEAAESE EDDNLSSMLH QRAEIPWRAC AKYLSSAGIL LLSLLVFSQL
LKHMVLVAID YWLAKWTDSA LTLTPAARNC SLSQECTLDQ TVYAMVFTVL CSLGIVLCLV
TSVTVEWTGL KVAKRLHRSL LNRIILAPMR FFETTPLGSI LNRFSSDCNT IDQHIPSTLE
CLSRSTLLCV SALAVISYVT PVFLVALLPL AIVCYFIQKY FRVASRDLQQ LDDTTQLPLL
SHFAETVEGL TTIRAFRYEA RFQQKLLEYT DSNNIASLFL TAANRWLEVR MEYIGACVVL
IAAVTSISNS LHRELSAGLV GLGLTYALMV SNYLNWMVRN LADMELQLGA VKRIHGLLKT
EAESYEGLLA PSLIPKNWPD QGKIQIQNLS VRYDSSLKPV LKHVNALIAP GQKIGICGRT
GSGKSSFSLA FFRMVDTFEG HIIIDGIDIA KLPLHTLRSR LSIILQDPVL FSGTIRFNLD
PERKCSDSTL WEALEIAQLK LVVKALPGGL DAIITEGGEN FSQGQRQLFC LARAFVRKTS
IFIMDEATAS IDMATENILQ KVVMTAFADR TVVTIAHRVH TILSADLVIV LKRGAILEFD
KPEKLLSRKD SVFASFVRAD K


Related products :

Catalog number Product name Quantity
E1242h ELISA kit ABC1,ABC-1,ABCA1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,CERP,Cholesterol efflux regulatory protein,Homo sapiens,Human 96T
E1242h ELISA ABC1,ABC-1,ABCA1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,CERP,Cholesterol efflux regulatory protein,Homo sapiens,Human 96T
U1242h CLIA ABC1,ABC-1,ABCA1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,CERP,Cholesterol efflux regulatory protein,Homo sapiens,Human 96T
E1242m ELISA kit Abc1,ABC-1,Abca1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,Mouse,Mus musculus 96T
U1242m CLIA Abc1,ABC-1,Abca1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,Mouse,Mus musculus 96T
E1242m ELISA Abc1,ABC-1,Abca1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,Mouse,Mus musculus 96T
20-372-60004 ATP-binding cassette - Mouse monoclonal anti-human ABCF_ antibody; ATP-binding cassette. sub-family F (GCN20). member 1. isoform CRA_a; ABC50 protein Monoclonal 0.1 mg
E1181h ELISA kit ABC transporter 9 protein,ABCB9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,hABCB9,Homo sapiens,Human,KIAA1520,TAPL,TAP-like protein 96T
U1181h CLIA ABC transporter 9 protein,ABCB9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,hABCB9,Homo sapiens,Human,KIAA1520,TAPL,TAP-like protein 96T
E1181h ELISA ABC transporter 9 protein,ABCB9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,hABCB9,Homo sapiens,Human,KIAA1520,TAPL,TAP-like protein 96T
U1181m CLIA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
E1181m ELISA kit ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
E1181m ELISA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
U1181r CLIA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
E1181r ELISA kit ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
E1181r ELISA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
EH1420 ATP-binding cassette sub-family A member 1 Elisa Kit 96T
CG47 ATP-binding cassette sub-family B member 5 ABCB5 lmg
ABCD2_RAT Rat ELISA Kit FOR ATP-binding cassette sub-family D member 2 96T
EM796 ATP-binding cassette sub-family G member 3 Elisa Kit 96T
E14498h Rat ELISA Kit FOR ATP-binding cassette sub-family D member 3 96T
ABCC8_RAT Rat ELISA Kit FOR ATP-binding cassette sub-family C member 8 96T
EH1095 ATP-binding cassette sub-family G member 2 Elisa Kit 96T
EM552 ATP-binding cassette sub-family A member 1 Elisa Kit 96T
CG47 ATP-binding cassette sub-family B member 5 ABCB5 500


 

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

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





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




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

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

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

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

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

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

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




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






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






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

GENTAUR Poland Sp. z o.o.


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

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

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