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Hepatocyte nuclear factor 1-alpha (HNF-1-alpha) (HNF-1A) (Liver-specific transcription factor LF-B1) (LFB1) (Transcription factor 1) (TCF-1)

 HNF1A_HUMAN             Reviewed;         631 AA.
P20823; A5Z2R8; E0YMJ5; E0YMK0; E0YMK1; E2I9R4; E2I9R5; F5H5U3;
Q2M3H2; Q99861;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
27-SEP-2017, entry version 211.
RecName: Full=Hepatocyte nuclear factor 1-alpha;
Short=HNF-1-alpha;
Short=HNF-1A;
AltName: Full=Liver-specific transcription factor LF-B1;
Short=LFB1;
AltName: Full=Transcription factor 1;
Short=TCF-1;
Name=HNF1A; Synonyms=TCF1;
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 A).
TISSUE=Liver;
PubMed=1707031; DOI=10.1016/0888-7543(90)90238-P;
Bach I., Galcheva-Gargova Z., Mattei M.-G., Simon-Chazottes D.,
Guenet J.-L., Cereghini S., Yaniv M.;
"Cloning of human hepatic nuclear factor 1 (HNF1) and chromosomal
localization of its gene in man and mouse.";
Genomics 8:155-164(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND ALTERNATIVE SPLICING.
TISSUE=Liver;
PubMed=7900999;
Bach I., Yaniv M.;
"More potent transcriptional activators or a transdominant inhibitor
of the HNF1 homeoprotein family are generated by alternative RNA
processing.";
EMBO J. 12:4229-4242(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MODY3 LEU-447.
PubMed=8945470; DOI=10.1038/384455a0;
Yamagata K., Oda N., Kaisaki P.J., Menzel S., Furuta H.,
Vaxillaire M., Southam L., Cox R.D., Lathrop G.M., Boriraj V.V.,
Chen X., Cox N.J., Oda Y., Yano H., le Beau M.M., Yamada S.,
Nishigori H., Takeda J., Fajans S.S., Hattersley A.T., Iwasaki N.,
Hansen T., Pedersen O., Polonsky K.S., Turner R.C., Velho G.,
Chevre J.-C., Froguel P., Bell G.I.;
"Mutations in the hepatocyte nuclear factor-1alpha gene in maturity-
onset diabetes of the young (MODY3).";
Nature 384:455-458(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6).
Yang C.-W., Tsai D.-Y.;
"Homo sapiens HNF1 alpha B mRNA splicing variants.";
Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND VARIANT SER-574.
Gonzalez Ruano E., Gonzalez Sarmiento R.;
"New isoforms in HNF1A.";
Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-27; VAL-98;
ASN-487 AND SER-574.
SeattleSNPs variation discovery resource;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-27.
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-247, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 85-278 IN COMPLEX WITH DNA,
FUNCTION, DNA-BINDING, MUTAGENESIS OF ASN-127; GLU-132; PHE-177;
ILE-186; THR-190; ASN-202; VAL-246 AND ASN-257, AND CHARACTERIZATION
OF VARIANTS MODY3 PHE-142 AND GLN-205.
PubMed=12453420; DOI=10.1016/S1097-2765(02)00704-9;
Chi Y.I., Frantz J.D., Oh B.C., Hansen L., Dhe-Paganon S.,
Shoelson S.E.;
"Diabetes mutations delineate an atypical POU domain in HNF-1alpha.";
Mol. Cell 10:1129-1137(2002).
[12]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-32, AND CIRCULAR DICHROISM.
PubMed=16930618; DOI=10.1016/j.jmb.2006.06.086;
Narayana N., Phillips N.B., Hua Q.X., Jia W., Weiss M.A.;
"Diabetes mellitus due to misfolding of a beta-cell transcription
factor: stereospecific frustration of a Schellman motif in HNF-
1alpha.";
J. Mol. Biol. 362:414-429(2006).
[13]
VARIANTS MODY3 ARG-107; TRP-131; MET-260 AND HIS-272.
PubMed=9166684; DOI=10.2337/diab.46.6.1081;
Glucksmann M.A., Lehto M., Tayber O., Scotti S., Berkemeier L.,
Pulido J.C., Wu Y., Nir W.-J., Fang L., Markel P., Munnelly K.D.,
Goranson J., Orho M., Young B.M., Whitacre J.L., McMenimen C.,
Wantman M., Tuomi T., Warram J., Forsblom C.M., Carlsson M.,
Rosenzweig J., Kennedy G., Duyk G.M., Krolewski A.S., Groop L.C.,
Thomas J.D.;
"Novel mutations and a mutational hotspot in the MODY3 gene.";
Diabetes 46:1081-1086(1997).
[14]
VARIANTS MODY3 HIS-12; GLN-131; GLN-205 AND CYS-263, AND VARIANT NIDDM
ASP-191.
PubMed=9287053; DOI=10.2337/diab.46.9.1504;
Iwasaki N., Oda N., Ogata M., Hara M., Hinokio Y., Oda Y.,
Yamagata K., Kanematsu S., Ohgawara H., Omori Y., Bell G.I.;
"Mutations in the hepatocyte nuclear factor-1alpha/MODY3 gene in
Japanese subjects with early- and late-onset NIDDM.";
Diabetes 46:1504-1508(1997).
[15]
VARIANT NIDDM MET-254, AND VARIANTS LEU-27 AND ASN-487.
PubMed=9287055; DOI=10.2337/diab.46.9.1512;
Yamada S., Nishigori H., Onda H., Takahashi K., Kitano N.,
Morikawa A., Takeuchi T., Takeda J.;
"Mutations in the hepatocyte nuclear factor-1alpha gene (MODY3) are
not a major cause of late-onset NIDDM in Japanese subjects.";
Diabetes 46:1512-1513(1997).
[16]
VARIANTS IDDM20 HIS-272 AND GLY-583.
PubMed=9313763; DOI=10.2337/diacare.46.10.1643;
Yamada S., Nishigori H., Onda H., Utsugi T., Yanagawa T., Maruyama T.,
Onigata K., Nagashima K., Nagai R., Morikawa A., Takeuchi T.,
Takeda J.;
"Identification of mutations in the hepatocyte nuclear factor (HNF)-1-
alpha gene in Japanese subjects with IDDM.";
Diabetes 46:1643-1647(1997).
[17]
VARIANTS MODY3, AND VARIANT ATYPICAL DIABETES SER-574.
PubMed=9392505; DOI=10.2337/diab.46.12.2108;
Boutin P., Chevre J.-C., Hani E.H., Gomis R., Pardini V.C.,
Guillausseau P.-J., Vaxillaire M., Velho G., Froguel P.;
"An automated fluorescent single-strand conformation polymorphism
technique for screening mutations in the hepatocyte nuclear factor-
1alpha gene (maturity-onset diabetes of the young).";
Diabetes 46:2108-2109(1997).
[18]
VARIANTS MODY3 GLN-131; GLN-229; GLY-241 AND HIS-272.
PubMed=9032114; DOI=10.2337/diab.46.3.528;
Kaisaki P.J., Menzel S., Lindner T., Oda N., Rjasanowski I., Sahm J.,
Meincke G., Schulze J., Schmechel H., Petzold C., Ledermann H.M.,
Sachse G., Boriraj V.V., Menzel R., Kerner W., Turner R.C.,
Yamagata K., Bell G.I.;
"Mutations in the hepatocyte nuclear factor-1alpha gene in MODY and
early-onset NIDDM: evidence for a mutational hotspot in exon 4.";
Diabetes 46:528-535(1997).
[19]
VARIANTS MODY3 THR-129; TRP-131; TRP-159; LEU-519 AND ILE-620.
PubMed=9075818; DOI=10.2337/diab.46.4.720;
Frayling T.M., Bulman M.P., Ellard S., Appleton M., Dronsfield M.J.,
Mackie A.D., Baird J.D., Kaisaki P.J., Yamagata K., Bell G.I.,
Bain S.C., Hattersley A.T.;
"Mutations in the hepatocyte nuclear factor-1alpha gene are a common
cause of maturity-onset diabetes of the young in the U.K.";
Diabetes 46:720-725(1997).
[20]
VARIANTS MODY3 ASN-128; TYR-143 AND LEU-447.
PubMed=9075819; DOI=10.2337/diab.46.4.726;
Hansen T., Eiberg H., Rouard M., Vaxillaire M., Moeller A.M.,
Rasmussen S.K., Fridberg M., Urhammer S.A., Holst J.J., Almind K.,
Echwald S.M., Hansen L., Bell G.I., Pedersen O.;
"Novel MODY3 mutations in the hepatocyte nuclear factor-1alpha gene:
evidence for a hyperexcitability of pancreatic beta-cells to
intravenous secretagogues in a glucose-tolerant carrier of a P447L
mutation.";
Diabetes 46:726-730(1997).
[21]
VARIANTS LEU-27; VAL-98 AND ASN-487.
PubMed=9133564; DOI=10.2337/diab.46.5.912;
Urhammer S.A., Fridberg M., Hansen T., Rasmussen S.K., Moeller A.M.,
Clausen J.O., Pedersen O.;
"A prevalent amino acid polymorphism at codon 98 in the hepatocyte
nuclear factor-1alpha gene is associated with reduced serum C-peptide
and insulin responses to an oral glucose challenge.";
Diabetes 46:912-916(1997).
[22]
VARIANT NIDDM GLN-583, AND VARIANTS LEU-27; VAL-98 AND ASN-487.
PubMed=9112026; DOI=10.1007/s001250050703;
Urhammer S.A., Rasmussen S.K., Kaisaki P.J., Oda N., Yamagata K.,
Moeller A.M., Fridberg M., Hansen L., Hansen T., Bell G.I.,
Pedersen O.;
"Genetic variation in the hepatocyte nuclear factor-1 alpha gene in
Danish Caucasians with late-onset NIDDM.";
Diabetologia 40:473-475(1997).
[23]
VARIANTS MODY3 CYS-122; PHE-142 AND GLN-159.
PubMed=9097962; DOI=10.1093/hmg/6.4.583;
Vaxillaire M., Rouard M., Yamagata K., Oda N., Kaisaki P.J.,
Boriraj V.V., Chevre J.-C., Boccio V., Cox R.D., Lathrop G.M.,
Dussoix P., Philippe J., Timsit J., Charpentier G., Velho G.,
Bell G.I., Froguel P.;
"Identification of nine novel mutations in the hepatocyte nuclear
factor 1 alpha gene associated with maturity-onset diabetes of the
young (MODY3).";
Hum. Mol. Genet. 6:583-586(1997).
[24]
VARIANTS LEU-27; ASN-487 AND ARG-514.
PubMed=9604876; DOI=10.2337/diabetes.47.6.967;
Behn P.S., Wasson J., Chayen S., Smolovitch I., Thomas J.D.,
Glaser B., Permutt M.A.;
"Hepatocyte nuclear factor 1alpha coding mutations are an uncommon
contributor to early-onset type 2 diabetes in Ashkenazi Jews.";
Diabetes 47:967-969(1998).
[25]
VARIANTS MODY3 ASP-31; TRP-159; THR-161; TRP-200 AND TRP-271.
PubMed=9754819; DOI=10.1007/s001250051025;
Chevre J.-C., Hani E.H., Boutin P., Vaxillaire M., Blanche H.,
Vionnet N., Pardini V.C., Timsit J., Larger E., Charpentier G.,
Beckers D., Maes M., Bellanne-Chantelot C., Velho G., Froguel P.;
"Mutation screening in 18 Caucasian families suggest the existence of
other MODY genes.";
Diabetologia 41:1017-1023(1998).
[26]
VARIANTS IDDM20 LYS-48 AND GLY-241.
PubMed=9867222; DOI=10.1007/s001250051101;
Moeller A.M., Dalgaard L.T., Pociot F., Nerup J., Hansen T.,
Pedersen O.;
"Mutations in the hepatocyte nuclear factor-1alpha gene in Caucasian
families originally classified as having type I diabetes.";
Diabetologia 41:1528-1531(1998).
[27]
VARIANTS MODY3 ARG-537 AND LYS-619.
PubMed=9626139; DOI=10.1210/jcem.83.6.4874;
Elbein S.C., Teng K., Yount P., Scroggin E.;
"Linkage and molecular scanning analyses of MODY3/hepatocyte nuclear
factor-1 alpha gene in typical familial type 2 diabetes: evidence for
novel mutations in exons 8 and 10.";
J. Clin. Endocrinol. Metab. 83:2059-2065(1998).
[28]
VARIANTS LEU-27 AND ASN-487.
PubMed=9621514; DOI=10.1007/s100380050049;
Nishigori H., Yamada S., Kohama T., Utsugi T., Shimizu H.,
Takeuchi T., Takeda J.;
"Mutations in the hepatocyte nuclear factor-1 alpha gene 'MODY3' are
not a major cause of early-onset non-insulin-dependent 'type 2'
diabetes mellitus in Japanese.";
J. Hum. Genet. 43:107-110(1998).
[29]
VARIANTS MODY3 HIS-12; ASN-158; GLN-159 AND CYS-203.
PubMed=10078571; DOI=10.2337/diabetes.48.3.645;
Yamada S., Tomura H., Nishigori H., Sho K., Mabe H., Iwatani N.,
Takumi T., Kito Y., Moriya N., Muroya K., Ogata T., Onigata K.,
Morikawa A., Inoue I., Takeda J.;
"Identification of mutations in the hepatocyte nuclear factor-1alpha
gene in Japanese subjects with early-onset NIDDM and functional
analysis of the mutant proteins.";
Diabetes 48:645-648(1999).
[30]
VARIANTS MODY3 GLU-117 AND TYR-143.
PubMed=10102714; DOI=10.2337/diabetes.48.4.921;
Ellard S., Bulman M.P., Frayling T.M., Allen L.I.S., Dronsfield M.J.,
Tack C.J., Hattersley A.T.;
"Allelic drop-out in exon 2 of the hepatocyte nuclear factor-1alpha
gene hinders the identification of mutations in three families with
maturity-onset diabetes of the young.";
Diabetes 48:921-923(1999).
[31]
VARIANT NIDDM CYS-272, AND VARIANT IDDM20 ARG-415.
PubMed=10333057; DOI=10.1007/s001250051204;
Yoshiuchi I., Yamagata K., Yang Q., Iwahashi H., Okita K.,
Yamamoto K., Oue T., Imagawa A., Hamaguchi T., Yamasaki T.,
Horikawa Y., Satoh T., Nakajima H., Miyazaki J., Higashiyama S.,
Miyagawa J., Namba M., Hanafusa T., Matsuzawa Y.;
"Three new mutations in the hepatocyte nuclear factor-1alpha gene in
Japanese subjects with diabetes mellitus: clinical features and
functional characterization.";
Diabetologia 42:621-626(1999).
[32]
VARIANTS MODY3 ARG-20; HIS-203; CYS-432 AND MET-618.
PubMed=10588527; DOI=10.1046/j.1464-5491.1999.00188.x;
Ng M.C.Y., Cockburn B.N., Lindner T.H., Yeung V.T.F., Chow C.-C.,
So W.-Y., Li J.K.Y., Lo Y.M.D., Lee Z.S.K., Cockram C.S.,
Critchley J.A.J.H., Bell G.I., Chan J.C.N.;
"Molecular genetics of diabetes mellitus in Chinese subjects:
identification of mutations in glucokinase and hepatocyte nuclear
factor-1alpha genes in patients with early-onset type 2 diabetes
mellitus/MODY.";
Diabet. Med. 16:956-963(1999).
[33]
VARIANT MODY3 ILE-620.
PubMed=10482964; DOI=10.1038/sj.ejhg.5200358;
Miedzybrodzka Z., Hattersley A.T., Ellard S., Pearson D., de Silva D.,
Harvey R., Haites N.;
"Non-penetrance in a MODY 3 family with a mutation in the hepatic
nuclear factor 1alpha gene: implications for predictive testing.";
Eur. J. Hum. Genet. 7:729-732(1999).
[34]
VARIANT SER-319.
PubMed=10084598; DOI=10.1210/jcem.84.3.5528;
Hegele R.A., Cao H., Harris S.B., Hanley A.J.G., Zinman B.;
"The hepatic nuclear factor-1alpha G319S variant is associated with
early-onset type 2 diabetes in Canadian Oji-Cree.";
J. Clin. Endocrinol. Metab. 84:1077-1082(1999).
[35]
CHARACTERIZATION OF VARIANTS MODY3 HIS-12; ARG-20 AND ASP-31,
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PCBD1.
PubMed=10966642; DOI=10.1038/78966;
Rose R.B., Bayle J.H., Endrizzi J.A., Cronk J.D., Crabtree G.R.,
Alber T.;
"Structural basis of dimerization, coactivator recognition and MODY3
mutations in HNF-1alpha.";
Nat. Struct. Biol. 7:744-748(2000).
[36]
INVOLVEMENT IN HEPATIC ADENOMAS, AND VARIANTS TYR-127; CYS-165;
CYS-206; LEU-206; SER-237; GLY-244; PRO-250; CYS-268; GLU-273; SER-574
AND GLN-583.
PubMed=12355088; DOI=10.1038/ng1001;
Bluteau O., Jeannot E., Bioulac-Sage P., Marques J.M., Blanc J.-F.,
Bui H., Beaudoin J.-C., Franco D., Balabaud C., Laurent-Puig P.,
Zucman-Rossi J.;
"Bi-allelic inactivation of TCF1 in hepatic adenomas.";
Nat. Genet. 32:312-315(2002).
[37]
VARIANT [LARGE SCALE ANALYSIS] GLU-273.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Transcriptional activator that regulates the tissue
specific expression of multiple genes, especially in pancreatic
islet cells and in liver. Required for the expression of several
liver specific genes. Binds to the inverted palindrome 5'-
GTTAATNATTAAC-3'. {ECO:0000269|PubMed:10966642,
ECO:0000269|PubMed:12453420}.
-!- SUBUNIT: Binds DNA as a dimer. Interacts with PCBD1.
Heterotetramer with PCBD1; formed by a dimer of dimers.
{ECO:0000269|PubMed:10966642, ECO:0000269|PubMed:12453420}.
-!- INTERACTION:
Q9Y463:DYRK1B; NbExp=4; IntAct=EBI-636034, EBI-634187;
P61457:PCBD1; NbExp=2; IntAct=EBI-636034, EBI-740475;
Q9H0N5:PCBD2; NbExp=2; IntAct=EBI-636034, EBI-634289;
Q92786:PROX1; NbExp=3; IntAct=EBI-636034, EBI-3912635;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00108, ECO:0000269|PubMed:10966642}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=A;
IsoId=P20823-1; Sequence=Displayed;
Name=B;
IsoId=P20823-2; Sequence=VSP_002250, VSP_002251;
Name=C;
IsoId=P20823-3; Sequence=VSP_002252, VSP_002253;
Name=4;
IsoId=P20823-4; Sequence=VSP_047736, VSP_047739;
Name=5;
IsoId=P20823-5; Sequence=VSP_047737, VSP_047738;
Name=6;
IsoId=P20823-6; Sequence=VSP_053324, VSP_053325, VSP_053326;
Name=7; Synonyms=insIVS8;
IsoId=P20823-7; Sequence=VSP_054302;
Note=Due to intron retention. Ref.5 (ADK56177) sequence is in
conflict in position: 551:L->S. {ECO:0000305};
Name=8; Synonyms=delta 2;
IsoId=P20823-8; Sequence=VSP_054300, VSP_054301;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Liver.
-!- POLYMORPHISM: The Ala-98/Val-98 polymorphism is associated with a
reduction in glucose-induced serum C-peptide and insulin
responses. {ECO:0000269|PubMed:9133564}.
-!- DISEASE: Hepatic adenomas familial (HEPAF) [MIM:142330]: Rare
benign liver tumors of presumable epithelial origin that develop
in an otherwise normal liver. Hepatic adenomas may be single or
multiple. They consist of sheets of well-differentiated
hepatocytes that contain fat and glycogen and can produce bile.
Bile ducts or portal areas are absent. Kupffer cells, if present,
are reduced in number and are non-functional. Conditions
associated with adenomas are insulin-dependent diabetes mellitus
and glycogen storage diseases (types 1 and 3). Note=The disease is
caused by mutations affecting the gene represented in this entry.
Bi-allelic inactivation of HNF1A, whether sporadic or associated
with MODY3, may be an early step in the development of some
hepatocellular carcinomas.
-!- DISEASE: Maturity-onset diabetes of the young 3 (MODY3)
[MIM:600496]: A form of diabetes that is characterized by an
autosomal dominant mode of inheritance, onset in childhood or
early adulthood (usually before 25 years of age), a primary defect
in insulin secretion and frequent insulin-independence at the
beginning of the disease. {ECO:0000269|PubMed:10078571,
ECO:0000269|PubMed:10102714, ECO:0000269|PubMed:10482964,
ECO:0000269|PubMed:10588527, ECO:0000269|PubMed:10966642,
ECO:0000269|PubMed:12453420, ECO:0000269|PubMed:8945470,
ECO:0000269|PubMed:9032114, ECO:0000269|PubMed:9075818,
ECO:0000269|PubMed:9075819, ECO:0000269|PubMed:9097962,
ECO:0000269|PubMed:9166684, ECO:0000269|PubMed:9287053,
ECO:0000269|PubMed:9392505, ECO:0000269|PubMed:9626139,
ECO:0000269|PubMed:9754819}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Diabetes mellitus, insulin-dependent, 20 (IDDM20)
[MIM:612520]: A multifactorial disorder of glucose homeostasis
that is characterized by susceptibility to ketoacidosis in the
absence of insulin therapy. Clinical features are polydipsia,
polyphagia and polyuria which result from hyperglycemia-induced
osmotic diuresis and secondary thirst. These derangements result
in long-term complications that affect the eyes, kidneys, nerves,
and blood vessels. {ECO:0000269|PubMed:10333057,
ECO:0000269|PubMed:9313763, ECO:0000269|PubMed:9867222}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the HNF1 homeobox family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Hepatocyte nuclear factors
entry;
URL="https://en.wikipedia.org/wiki/Hepatocyte_nuclear_factors";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tcf1/";
-----------------------------------------------------------------------
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EMBL; M57732; AAA88077.1; -; mRNA.
EMBL; X71346; CAB59201.1; -; mRNA.
EMBL; U72618; AAC51137.1; -; Genomic_DNA.
EMBL; U72612; AAC51137.1; JOINED; Genomic_DNA.
EMBL; U72613; AAC51137.1; JOINED; Genomic_DNA.
EMBL; U72614; AAC51137.1; JOINED; Genomic_DNA.
EMBL; U72615; AAC51137.1; JOINED; Genomic_DNA.
EMBL; U72616; AAC51137.1; JOINED; Genomic_DNA.
EMBL; U72617; AAC51137.1; JOINED; Genomic_DNA.
EMBL; HM116552; ADM43489.1; -; mRNA.
EMBL; HM116557; ADM43494.1; -; mRNA.
EMBL; HM116558; ADM43495.1; -; mRNA.
EMBL; HM449088; ADK56177.1; -; mRNA.
EMBL; HM449089; ADK56178.1; -; mRNA.
EMBL; EF641294; ABR09270.1; -; Genomic_DNA.
EMBL; AC079602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW98226.1; -; Genomic_DNA.
EMBL; BC104908; AAI04909.1; -; mRNA.
EMBL; BC104910; AAI04911.1; -; mRNA.
CCDS; CCDS9209.1; -. [P20823-1]
PIR; A36749; A36749.
RefSeq; NP_000536.5; NM_000545.6. [P20823-1]
RefSeq; NP_001293108.1; NM_001306179.1.
UniGene; Hs.654455; -.
PDB; 1IC8; X-ray; 2.60 A; A/B=85-278.
PDB; 2GYP; X-ray; 1.40 A; A/B=2-32.
PDBsum; 1IC8; -.
PDBsum; 2GYP; -.
ProteinModelPortal; P20823; -.
SMR; P20823; -.
BioGrid; 112789; 39.
DIP; DIP-33544N; -.
IntAct; P20823; 14.
STRING; 9606.ENSP00000257555; -.
DrugBank; DB04419; Norleucine.
iPTMnet; P20823; -.
PhosphoSitePlus; P20823; -.
BioMuta; HNF1A; -.
DMDM; 51338763; -.
MaxQB; P20823; -.
PaxDb; P20823; -.
PeptideAtlas; P20823; -.
PRIDE; P20823; -.
DNASU; 6927; -.
Ensembl; ENST00000538646; ENSP00000443964; ENSG00000135100. [P20823-4]
Ensembl; ENST00000540108; ENSP00000445445; ENSG00000135100. [P20823-8]
Ensembl; ENST00000541924; ENSP00000440361; ENSG00000135100. [P20823-5]
GeneID; 6927; -.
KEGG; hsa:6927; -.
UCSC; uc021rfb.2; human. [P20823-1]
CTD; 6927; -.
DisGeNET; 6927; -.
EuPathDB; HostDB:ENSG00000135100.17; -.
GeneCards; HNF1A; -.
H-InvDB; HIX0036847; -.
HGNC; HGNC:11621; HNF1A.
HPA; HPA035231; -.
MalaCards; HNF1A; -.
MIM; 142330; phenotype.
MIM; 142410; gene.
MIM; 600496; phenotype.
MIM; 606391; phenotype.
MIM; 612520; phenotype.
neXtProt; NX_P20823; -.
OpenTargets; ENSG00000135100; -.
Orphanet; 324575; Hyperinsulinism due to HNF1A deficiency.
Orphanet; 552; MODY.
PharmGKB; PA36380; -.
eggNOG; ENOG410IFA0; Eukaryota.
eggNOG; ENOG410ZZZ0; LUCA.
GeneTree; ENSGT00860000133745; -.
HOGENOM; HOG000015305; -.
HOVERGEN; HBG005980; -.
InParanoid; P20823; -.
KO; K08036; -.
PhylomeDB; P20823; -.
TreeFam; TF320327; -.
Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
SignaLink; P20823; -.
SIGNOR; P20823; -.
EvolutionaryTrace; P20823; -.
GeneWiki; HNF1A; -.
GenomeRNAi; 6927; -.
PRO; PR:P20823; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135100; -.
CleanEx; HS_HNF1A; -.
ExpressionAtlas; P20823; baseline and differential.
Genevisible; P20823; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0046323; P:glucose import; IMP:UniProtKB.
GO; GO:0030073; P:insulin secretion; IMP:UniProtKB.
GO; GO:0001779; P:natural killer cell differentiation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IGI:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0035623; P:renal glucose absorption; IMP:UniProtKB.
CDD; cd00086; homeodomain; 1.
InterPro; IPR006899; HNF-1_N.
InterPro; IPR023219; HNF1_dimer_dom.
InterPro; IPR006898; HNF1a_C.
InterPro; IPR006897; HNF1b_C.
InterPro; IPR009057; Homeobox-like.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR010982; Lambda_DNA-bd_dom.
Pfam; PF04814; HNF-1_N; 1.
Pfam; PF04813; HNF-1A_C; 1.
Pfam; PF04812; HNF-1B_C; 1.
Pfam; PF00046; Homeobox; 1.
SMART; SM00389; HOX; 1.
SUPFAM; SSF100957; SSF100957; 1.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF47413; SSF47413; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
Diabetes mellitus; Disease mutation; DNA-binding; Homeobox; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 631 Hepatocyte nuclear factor 1-alpha.
/FTId=PRO_0000049115.
DNA_BIND 199 279 Homeobox; HNF1-type.
{ECO:0000255|PROSITE-ProRule:PRU00108}.
REGION 1 31 Dimerization.
REGION 130 132 Interaction with DNA.
REGION 143 149 Interaction with DNA.
REGION 155 158 Interaction with DNA.
REGION 203 206 Interaction with DNA.
REGION 263 265 Interaction with DNA.
REGION 270 273 Interaction with DNA.
MOTIF 197 205 Nuclear localization signal.
{ECO:0000305}.
COMPBIAS 71 80 Asp/Glu-rich (acidic; potential
involvement with transcription).
MOD_RES 70 70 Phosphoserine.
{ECO:0000250|UniProtKB:P22361}.
MOD_RES 74 74 Phosphothreonine.
{ECO:0000250|UniProtKB:P22361}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 313 313 Phosphoserine.
{ECO:0000250|UniProtKB:P22361}.
VAR_SEQ 1 117 Missing (in isoform 6).
{ECO:0000303|Ref.4}.
/FTId=VSP_053324.
VAR_SEQ 110 119 EDPWRVAKMV -> VHPCRAGRAD (in isoform 8).
{ECO:0000305}.
/FTId=VSP_054300.
VAR_SEQ 120 631 Missing (in isoform 8). {ECO:0000305}.
/FTId=VSP_054301.
VAR_SEQ 176 278 QFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQ
AYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSN
LVTEVRVYNWFANRRKEEAFR -> RRNASREGCPHHRHRG
WAPTSSRRCVSTTGLPTGAKKKPSGTSWPWTRTAGPPQGQA
RDLRCPLTAPLACLHLPSPPVRSTVCAMDSLRPVRLQKYPQ
AAAVP (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_047736.
VAR_SEQ 239 247 AECIQRGVS -> CALWTACDQ (in isoform 5).
{ECO:0000303|Ref.4}.
/FTId=VSP_047737.
VAR_SEQ 248 631 Missing (in isoform 5).
{ECO:0000303|Ref.4}.
/FTId=VSP_047738.
VAR_SEQ 279 631 Missing (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_047739.
VAR_SEQ 438 520 LASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMP
PVQSHVTQSPFMATMAQLQSPHALYSHKPEVAQYTHTGLLP
Q -> KLVGMGGHLGGRLMGQPQNPGAGRATGTHSFIHTTC
IYPVPTLDQSLCYISDTWVNQTDQNLSNSSREAGTKHNTSI
LWYLRR (in isoform 6).
{ECO:0000303|Ref.4}.
/FTId=VSP_053325.
VAR_SEQ 438 494 LASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMP
PVQSHVTQSPFMATMA -> KLVGMGGHLGGRLMGQPQNPG
AGRATGTHSFIHSFIQHVFIQCLLWTSHCATSVIPG (in
isoform C). {ECO:0000305}.
/FTId=VSP_002252.
VAR_SEQ 495 601 Missing (in isoform C). {ECO:0000305}.
/FTId=VSP_002253.
VAR_SEQ 501 542 ALYSHKPEVAQYTHTGLLPQTMLITDTTNLSALASLTPTKQ
V -> GEHPVPHTAGDDDRGWLSMDAGERGAWQALQSACVS
GTSVFP (in isoform B). {ECO:0000305}.
/FTId=VSP_002250.
VAR_SEQ 521 631 Missing (in isoform 6).
{ECO:0000303|Ref.4}.
/FTId=VSP_053326.
VAR_SEQ 540 540 K -> KQVRSRPAGPPLACDRAPHPHIPRAQEAALLP (in
isoform 7). {ECO:0000303|Ref.5}.
/FTId=VSP_054302.
VAR_SEQ 543 601 Missing (in isoform B). {ECO:0000305}.
/FTId=VSP_002251.
VARIANT 12 12 L -> H (in MODY3; abolishes interaction
with PCBD1 and DNA).
{ECO:0000269|PubMed:10078571,
ECO:0000269|PubMed:10966642,
ECO:0000269|PubMed:9287053}.
/FTId=VAR_010537.
VARIANT 20 20 G -> R (in MODY3; abolishes interaction
with PCBD1 and DNA).
{ECO:0000269|PubMed:10588527,
ECO:0000269|PubMed:10966642}.
/FTId=VAR_012483.
VARIANT 27 27 I -> L (in dbSNP:rs1169288).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9112026,
ECO:0000269|PubMed:9133564,
ECO:0000269|PubMed:9287055,
ECO:0000269|PubMed:9604876,
ECO:0000269|PubMed:9621514,
ECO:0000269|Ref.6}.
/FTId=VAR_007905.
VARIANT 31 31 G -> D (in MODY3; no effect on
interaction with PCBD1 and DNA).
{ECO:0000269|PubMed:10966642,
ECO:0000269|PubMed:9754819}.
/FTId=VAR_010538.
VARIANT 48 48 E -> K (in IDDM20).
{ECO:0000269|PubMed:9867222}.
/FTId=VAR_010539.
VARIANT 98 98 A -> V (in dbSNP:rs1800574).
{ECO:0000269|PubMed:9112026,
ECO:0000269|PubMed:9133564,
ECO:0000269|Ref.6}.
/FTId=VAR_010540.
VARIANT 107 107 L -> R (in MODY3).
{ECO:0000269|PubMed:9166684}.
/FTId=VAR_010541.
VARIANT 117 117 K -> E (in MODY3).
{ECO:0000269|PubMed:10102714}.
/FTId=VAR_010542.
VARIANT 122 122 Y -> C (in MODY3).
{ECO:0000269|PubMed:9097962}.
/FTId=VAR_003756.
VARIANT 127 127 N -> Y (in a hepatocellular carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033088.
VARIANT 128 128 I -> N (in MODY3).
{ECO:0000269|PubMed:9075819}.
/FTId=VAR_010543.
VARIANT 129 129 P -> T (in MODY3).
{ECO:0000269|PubMed:9075818}.
/FTId=VAR_010544.
VARIANT 131 131 R -> Q (in MODY3; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:9032114,
ECO:0000269|PubMed:9287053}.
/FTId=VAR_010545.
VARIANT 131 131 R -> W (in MODY3; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:9075818,
ECO:0000269|PubMed:9166684}.
/FTId=VAR_010546.
VARIANT 133 133 V -> M (in MODY3).
/FTId=VAR_010547.
VARIANT 142 142 S -> F (in MODY3; reduces transcription
activation by about 80%).
{ECO:0000269|PubMed:12453420,
ECO:0000269|PubMed:9097962}.
/FTId=VAR_003757.
VARIANT 143 143 H -> Y (in MODY3; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:10102714,
ECO:0000269|PubMed:9075819}.
/FTId=VAR_010548.
VARIANT 158 158 K -> N (in MODY3; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:10078571}.
/FTId=VAR_010549.
VARIANT 159 159 R -> Q (in MODY3).
{ECO:0000269|PubMed:10078571,
ECO:0000269|PubMed:9097962}.
/FTId=VAR_003758.
VARIANT 159 159 R -> W (in MODY3).
{ECO:0000269|PubMed:9075818,
ECO:0000269|PubMed:9754819}.
/FTId=VAR_010550.
VARIANT 161 161 A -> T (in MODY3).
{ECO:0000269|PubMed:9754819}.
/FTId=VAR_010551.
VARIANT 165 165 W -> C (in a hepatocellular carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033089.
VARIANT 191 191 G -> D (in late-onset NIDDM).
{ECO:0000269|PubMed:9287053}.
/FTId=VAR_010552.
VARIANT 200 200 R -> W (in MODY3; expected to interfere
with nuclear localization).
{ECO:0000269|PubMed:9754819}.
/FTId=VAR_063069.
VARIANT 203 203 R -> C (in MODY3; expected to interfere
with nuclear localization and DNA
binding). {ECO:0000269|PubMed:10078571}.
/FTId=VAR_010554.
VARIANT 203 203 R -> H (in MODY3; expected to interfere
with nuclear localization and DNA
binding). {ECO:0000269|PubMed:10588527}.
/FTId=VAR_012484.
VARIANT 205 205 K -> Q (in MODY3; reduces transcription
activation by about 50%).
{ECO:0000269|PubMed:12453420,
ECO:0000269|PubMed:9287053}.
/FTId=VAR_010555.
VARIANT 206 206 W -> C (in a hepatic adenoma sample;
somatic mutation; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033090.
VARIANT 206 206 W -> L (in a hepatic adenoma sample;
somatic mutation; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033091.
VARIANT 229 229 R -> Q (in MODY3).
{ECO:0000269|PubMed:9032114}.
/FTId=VAR_010556.
VARIANT 237 237 N -> S (in a hepatic multiple adenoma
sample; somatic mutation).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033092.
VARIANT 241 241 C -> G (in IDDM20 and MODY3).
{ECO:0000269|PubMed:9032114,
ECO:0000269|PubMed:9867222}.
/FTId=VAR_010557.
VARIANT 244 244 R -> G (in a hepatic adenoma sample;
somatic mutation; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033093.
VARIANT 250 250 Q -> P (in a hepatocellular carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033094.
VARIANT 254 254 L -> M (in late-onset NIDDM; low
penetrance; unknown pathological
significance).
{ECO:0000269|PubMed:9287055}.
/FTId=VAR_010558.
VARIANT 259 259 V -> D (in MODY3).
/FTId=VAR_010559.
VARIANT 260 260 T -> M (in MODY3).
{ECO:0000269|PubMed:9166684}.
/FTId=VAR_010560.
VARIANT 263 263 R -> C (in MODY3; expected to interfere
with DNA binding).
{ECO:0000269|PubMed:9287053}.
/FTId=VAR_010561.
VARIANT 268 268 F -> C (in a hepatic adenoma sample;
somatic mutation).
{ECO:0000269|PubMed:12355088}.
/FTId=VAR_033095.
VARIANT 271 271 R -> W (in MODY3).
{ECO:0000269|PubMed:9754819}.
/FTId=VAR_010562.
VARIANT 272 272 R -> C (in NIDDM).
{ECO:0000269|PubMed:10333057}.
/FTId=VAR_010563.
VARIANT 272 272 R -> H (in IDDM20 and MODY3).
{ECO:0000269|PubMed:9032114,
ECO:0000269|PubMed:9166684,
ECO:0000269|PubMed:9313763}.
/FTId=VAR_003759.
VARIANT 273 273 K -> E (in a hepatic adenoma sample;
somatic mutation).
{ECO:0000269|PubMed:12355088,
ECO:0000269|PubMed:16959974}.
/FTId=VAR_033096.
VARIANT 319 319 G -> S (strong association with NIDDM
susceptibility; unique to the Canadian
Oji-Cree population).
{ECO:0000269|PubMed:10084598}.
/FTId=VAR_010564.
VARIANT 415 415 G -> R (in IDDM20; loss of function).
{ECO:0000269|PubMed:10333057}.
/FTId=VAR_010565.
VARIANT 432 432 S -> C (in MODY3).
{ECO:0000269|PubMed:10588527}.
/FTId=VAR_012485.
VARIANT 447 447 P -> L (in MODY3).
{ECO:0000269|PubMed:8945470,
ECO:0000269|PubMed:9075819}.
/FTId=VAR_003760.
VARIANT 487 487 S -> N (in dbSNP:rs2464196).
{ECO:0000269|PubMed:9112026,
ECO:0000269|PubMed:9133564,
ECO:0000269|PubMed:9287055,
ECO:0000269|PubMed:9604876,
ECO:0000269|PubMed:9621514,
ECO:0000269|Ref.6}.
/FTId=VAR_007906.
VARIANT 514 514 H -> R. {ECO:0000269|PubMed:9604876}.
/FTId=VAR_010566.
VARIANT 519 519 P -> L (in MODY3).
{ECO:0000269|PubMed:9075818}.
/FTId=VAR_010567.
VARIANT 537 537 T -> R (in MODY3; incomplete penetrance).
{ECO:0000269|PubMed:9626139}.
/FTId=VAR_010568.
VARIANT 574 574 G -> S (in a black African with an
atypical form of diabetes; also in an
individual with hepatic adenoma and
familial early-onset diabetes;
dbSNP:rs1169305).
{ECO:0000269|PubMed:12355088,
ECO:0000269|PubMed:9392505,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
/FTId=VAR_010569.
VARIANT 583 583 R -> G (in IDDM20).
{ECO:0000269|PubMed:9313763}.
/FTId=VAR_003761.
VARIANT 583 583 R -> Q (in late-onset NIDDM; also in an
individual with hepatic hyperplasia and
familial early-onset diabetes).
{ECO:0000269|PubMed:12355088,
ECO:0000269|PubMed:9112026}.
/FTId=VAR_010570.
VARIANT 594 594 S -> I (in MODY3).
/FTId=VAR_010571.
VARIANT 618 618 I -> M (in MODY3).
{ECO:0000269|PubMed:10588527}.
/FTId=VAR_012486.
VARIANT 619 619 E -> K (in MODY3).
{ECO:0000269|PubMed:9626139}.
/FTId=VAR_010572.
VARIANT 620 620 T -> I (in MODY3; incomplete penetrance).
{ECO:0000269|PubMed:10482964,
ECO:0000269|PubMed:9075818}.
/FTId=VAR_010573.
MUTAGEN 127 127 N->W: Abolishes transcription activation.
{ECO:0000269|PubMed:12453420}.
MUTAGEN 132 132 E->K: Abolishes transcription activation.
{ECO:0000269|PubMed:12453420}.
MUTAGEN 177 177 F->S: No significant effect on
transcription activation.
{ECO:0000269|PubMed:12453420}.
MUTAGEN 186 186 I->Q: No effect on transcription
activation.
{ECO:0000269|PubMed:12453420}.
MUTAGEN 190 190 T->Q: No effect on transcription
activation.
{ECO:0000269|PubMed:12453420}.
MUTAGEN 202 202 N->D: Reduces transcription activation by
70%. {ECO:0000269|PubMed:12453420}.
MUTAGEN 246 246 V->D: Reduces transcription activation by
75%. {ECO:0000269|PubMed:12453420}.
MUTAGEN 257 257 N->W: Reduces transcription activation by
70%. {ECO:0000269|PubMed:12453420}.
HELIX 4 19 {ECO:0000244|PDB:2GYP}.
HELIX 23 30 {ECO:0000244|PDB:2GYP}.
HELIX 94 107 {ECO:0000244|PDB:1IC8}.
HELIX 112 125 {ECO:0000244|PDB:1IC8}.
HELIX 130 137 {ECO:0000244|PDB:1IC8}.
HELIX 141 149 {ECO:0000244|PDB:1IC8}.
HELIX 156 169 {ECO:0000244|PDB:1IC8}.
TURN 170 173 {ECO:0000244|PDB:1IC8}.
HELIX 174 177 {ECO:0000244|PDB:1IC8}.
HELIX 208 221 {ECO:0000244|PDB:1IC8}.
TURN 226 229 {ECO:0000244|PDB:1IC8}.
HELIX 230 243 {ECO:0000244|PDB:1IC8}.
HELIX 255 257 {ECO:0000244|PDB:1IC8}.
HELIX 261 274 {ECO:0000244|PDB:1IC8}.
SEQUENCE 631 AA; 67356 MW; 8327CD4FDC39254A CRC64;
MVSKLSQLQT ELLAALLESG LSKEALIQAL GEPGPYLLAG EGPLDKGESC GGGRGELAEL
PNGLGETRGS EDETDDDGED FTPPILKELE NLSPEEAAHQ KAVVETLLQE DPWRVAKMVK
SYLQQHNIPQ REVVDTTGLN QSHLSQHLNK GTPMKTQKRA ALYTWYVRKQ REVAQQFTHA
GQGGLIEEPT GDELPTKKGR RNRFKWGPAS QQILFQAYER QKNPSKEERE TLVEECNRAE
CIQRGVSPSQ AQGLGSNLVT EVRVYNWFAN RRKEEAFRHK LAMDTYSGPP PGPGPGPALP
AHSSPGLPPP ALSPSKVHGV RYGQPATSET AEVPSSSGGP LVTVSTPLHQ VSPTGLEPSH
SLLSTEAKLV SAAGGPLPPV STLTALHSLE QTSPGLNQQP QNLIMASLPG VMTIGPGEPA
SLGPTFTNTG ASTLVIGLAS TQAQSVPVIN SMGSSLTTLQ PVQFSQPLHP SYQQPLMPPV
QSHVTQSPFM ATMAQLQSPH ALYSHKPEVA QYTHTGLLPQ TMLITDTTNL SALASLTPTK
QVFTSDTEAS SESGLHTPAS QATTLHVPSQ DPAGIQHLQP AHRLSASPTV SSSSLVLYQS
SDSSNGQSHL LPSNHSVIET FISTQMASSS Q


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