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Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)

 HNF4A_HUMAN             Reviewed;         474 AA.
P41235; A5JW41; B2RPP8; O00659; O00723; Q14540; Q5QPB8; Q6B4V5;
Q6B4V6; Q6B4V7; Q92653; Q92654; Q92655; Q99864; Q9NQH0;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 3.
27-SEP-2017, entry version 204.
RecName: Full=Hepatocyte nuclear factor 4-alpha;
Short=HNF-4-alpha;
AltName: Full=Nuclear receptor subfamily 2 group A member 1;
AltName: Full=Transcription factor 14;
Short=TCF-14;
AltName: Full=Transcription factor HNF-4;
Name=HNF4A; Synonyms=HNF4, NR2A1, TCF14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HNF4-ALPHA-1; HNF4-ALPHA-2 AND
HNF4-ALPHA-3), AND VARIANT SER-445.
TISSUE=Liver;
PubMed=8964514; DOI=10.1016/0378-1119(96)00183-7;
Kritis A.A., Argyrokastritis A., Moschonas N.K., Power S.,
Katrakili N., Zannis V.I., Cereghini S., Talianidis I.;
"Isolation and characterization of a third isoform of human hepatocyte
nuclear factor 4.";
Gene 173:275-280(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Kidney;
PubMed=8622695; DOI=10.1128/MCB.16.3.925;
Drewes T., Senkel S., Holewa B., Ryffel G.U.;
"Human hepatocyte nuclear factor 4 isoforms are encoded by distinct
and differentially expressed genes.";
Mol. Cell. Biol. 16:925-931(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8945471; DOI=10.1038/384458a0;
Yamagata K., Furuta H., Oda N., Kaisaki P.J., Menzel S., Cox N.J.,
Fajans S.S., Signorini S., Stoffel M., Bell G.I.;
"Mutations in the hepatocyte nuclear factor-4alpha gene in maturity-
onset diabetes of the young (MODY1).";
Nature 384:458-460(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE PROMOTER USAGE (ISOFORMS
HNF4-ALPHA-7; HNF4-ALPHA-8 AND HNF4-ALPHA-9).
Tanaka T., Jiang S., Hotta H., Takano K., Iwanari H., Hirayama Y.,
Midorikawa Y., Hippo Y., Watanabe A., Yamashita H., Kumakura J.,
Uchiyama Y., Hasegawa G., Aburatani H., Hamakubo T., Naito M.,
Sakai J., Kodama T.;
"Variation in P1 and P2 promoter-driven hepatocyte nuclear factor-4a
(HNF4a) expression in human tissues: implications for
carcinogenesis.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-139 AND ILE-453.
SeattleSNPs variation discovery resource;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HNF4-ALPHA-3).
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-474, AND ALTERNATIVE SPLICING.
TISSUE=Liver;
PubMed=7926813; DOI=10.1016/0378-1119(94)90079-5;
Chartier F.L., Bossu J.-P., Laudet V., Fruchart J.-C., Laine B.;
"Cloning and sequencing of cDNAs encoding the human hepatocyte nuclear
factor 4 indicate the presence of two isoforms in human liver.";
Gene 147:269-272(1994).
[10]
PHOSPHORYLATION.
PubMed=7568236; DOI=10.1073/pnas.92.21.9876;
Ktistaki E., Ktistakis N.T., Papadogeorgaki E., Talianidis I.;
"Recruitment of hepatocyte nuclear factor 4 into specific intranuclear
compartments depends on tyrosine phosphorylation that affects its DNA-
binding and transactivation potential.";
Proc. Natl. Acad. Sci. U.S.A. 92:9876-9880(1995).
[11]
PHOSPHORYLATION AT SER-313, AND MUTAGENESIS OF SER-313.
PubMed=12740371; DOI=10.1074/jbc.M304112200;
Hong Y.H., Varanasi U.S., Yang W., Leff T.;
"AMP-activated protein kinase regulates HNF4alpha transcriptional
activity by inhibiting dimer formation and decreasing protein
stability.";
J. Biol. Chem. 278:27495-27501(2003).
[12]
PHOSPHORYLATION AT SER-142; THR-166; SER-167; THR-432 AND SER-436,
UBIQUITINATION AT LYS-234 AND LYS-307, AND ACETYLATION AT LYS-458.
PubMed=21708125; DOI=10.1016/j.bbrc.2011.06.033;
Yokoyama A., Katsura S., Ito R., Hashiba W., Sekine H., Fujiki R.,
Kato S.;
"Multiple post-translational modifications in hepatocyte nuclear
factor 4alpha.";
Biochem. Biophys. Res. Commun. 410:749-753(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144; THR-429; THR-432
AND SER-436, 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).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 142-378, AND FATTY ACID
BINDING.
PubMed=14982928; DOI=10.1074/jbc.M400864200;
Duda K., Chi Y.-I., Shoelson S.E.;
"Structural basis for HNF-4alpha activation by ligand and coactivator
binding.";
J. Biol. Chem. 279:23311-23316(2004).
[15]
VARIANT MODY1 TRP-136.
PubMed=9313765; DOI=10.2337/diacare.46.10.1652;
Furuta H., Iwasaki N., Oda N., Hinokio Y., Horikawa Y., Yamagata K.,
Yano N., Sugahiro J., Ogata M., Ohgawara H., Omori Y., Iwamoto Y.,
Bell G.I.;
"Organization and partial sequence of the hepatocyte nuclear factor-4-
alpha/MODY1 gene and identification of a missense mutation, R127W, in
a Japanese family with MODY.";
Diabetes 46:1652-1657(1997).
[16]
VARIANT MODY1 GLN-285.
PubMed=9243109; DOI=10.1007/s001250050760;
Bulman M.P., Dronsfield M.J., Frayling T.M., Appleton M., Bain S.C.,
Ellard S., Hattersley A.T.;
"A missense mutation in the hepatocyte nuclear factor 4 alpha gene in
a UK pedigree with maturity-onset diabetes of the young.";
Diabetologia 40:859-862(1997).
[17]
VARIANTS ILE-139 AND MET-264.
PubMed=9267996; DOI=10.1007/s001250050778;
Moeller A.M., Urhammer S.A., Dalgaard L.T., Reneland R., Berglund L.,
Hansen T., Clausen J.O., Lithell H., Pedersen O.;
"Studies of the genetic variability of the coding region of the
hepatocyte nuclear factor-4alpha in Caucasians with maturity onset
NIDDM.";
Diabetologia 40:980-983(1997).
[18]
VARIANT NIDDM ILE-402.
PubMed=9449683; DOI=10.1172/JCI1403;
Hani E.H., Suaud L., Boutin P., Chevre J.-C., Durand E., Philippi A.,
Demenais F., Vionnet N., Furuta H., Velho G., Bell G.I., Laine B.,
Froguel P.;
"A missense mutation in hepatocyte nuclear factor-4-alpha, resulting
in a reduced transactivation activity, in human late-onset non-
insulin-dependent diabetes mellitus.";
J. Clin. Invest. 101:521-526(1998).
[19]
CHARACTERIZATION OF VARIANT MET-264, AND CHARACTERIZATION OF VARIANT
MODY1 GLN-285.
PubMed=10389854; DOI=10.2337/diabetes.48.7.1459;
Navas M.A., Munoz-Elias E.J., Kim J., Shih D., Stoffel M.;
"Functional characterization of the MODY1 gene mutations HNF4(R127W),
HNF4(V255M), and HNF4(E276Q).";
Diabetes 48:1459-1465(1999).
[20]
VARIANT MODY1 ARG-373.
PubMed=17407387; DOI=10.1371/journal.pmed.0040118;
Pearson E.R., Boj S.F., Steele A.M., Barrett T., Stals K.,
Shield J.P., Ellard S., Ferrer J., Hattersley A.T.;
"Macrosomia and hyperinsulinaemic hypoglycaemia in patients with
heterozygous mutations in the HNF4A gene.";
PLoS Med. 4:E118-E118(2007).
[21]
INVOLVEMENT IN FRTS4, AND VARIANT FRTS4 TRP-85.
PubMed=22802087; DOI=10.1210/jc.2012-1356;
Stanescu D.E., Hughes N., Kaplan B., Stanley C.A., De Leon D.D.;
"Novel presentations of congenital hyperinsulinism due to mutations in
the MODY genes: HNF1A and HNF4A.";
J. Clin. Endocrinol. Metab. 97:E2026-2030(2012).
[22]
VARIANT FRTS4 TRP-85.
PubMed=24285859; DOI=10.1136/jmedgenet-2013-102066;
Hamilton A.J., Bingham C., McDonald T.J., Cook P.R., Caswell R.C.,
Weedon M.N., Oram R.A., Shields B.M., Shepherd M., Inward C.D.,
Hamilton-Shield J.P., Kohlhase J., Ellard S., Hattersley A.T.;
"The HNF4A R76W mutation causes atypical dominant Fanconi syndrome in
addition to a beta cell phenotype.";
J. Med. Genet. 51:165-169(2014).
-!- FUNCTION: Transcriptionally controlled transcription factor. Binds
to DNA sites required for the transcription of alpha 1-
antitrypsin, apolipoprotein CIII, transthyretin genes and HNF1-
alpha. May be essential for development of the liver, kidney and
intestine.
-!- SUBUNIT: Homodimerization is required for HNF4-alpha to bind to
its recognition site. Interacts with PER2.
-!- INTERACTION:
Q99967:CITED2; NbExp=3; IntAct=EBI-1049011, EBI-937732;
P11532:DMD; NbExp=3; IntAct=EBI-12690684, EBI-295827;
O14602:EIF1AY; NbExp=3; IntAct=EBI-12690684, EBI-286439;
A8MYZ6:FOXO6; NbExp=2; IntAct=EBI-1049011, EBI-8531039;
P04150:NR3C1; NbExp=2; IntAct=EBI-1049011, EBI-493507;
O43688:PLPP2; NbExp=3; IntAct=EBI-12690684, EBI-722017;
Q9UBK2:PPARGC1A; NbExp=4; IntAct=EBI-1049011, EBI-765486;
Q92786:PROX1; NbExp=3; IntAct=EBI-1049011, EBI-3912635;
P23246:SFPQ; NbExp=2; IntAct=EBI-1049011, EBI-355453;
Q12772:SREBF2; NbExp=2; IntAct=EBI-1049011, EBI-465059;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
Comment=Additional isoforms seem to exist.;
Name=HNF4-Alpha-1; Synonyms=HNF-4B;
IsoId=P41235-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=HNF4-Alpha-2; Synonyms=HNF4-A;
IsoId=P41235-2; Sequence=VSP_003674;
Note=Produced by alternative splicing of isoform HNF4-Alpha-1.;
Name=HNF4-Alpha-3; Synonyms=HNF4-C;
IsoId=P41235-3; Sequence=VSP_003675;
Note=Produced by alternative splicing of isoform HNF4-Alpha-1.;
Name=HNF4-Alpha-4;
IsoId=P41235-4; Sequence=VSP_003673;
Note=Produced by alternative splicing of isoform HNF4-Alpha-1.;
Name=HNF4-Alpha-7;
IsoId=P41235-5; Sequence=VSP_026030;
Note=Produced by alternative promoter usage.;
Name=HNF4-Alpha-8;
IsoId=P41235-6; Sequence=VSP_026030, VSP_003674;
Note=Produced by alternative splicing of isoform HNF4-Alpha-7.;
Name=HNF4-Alpha-9;
IsoId=P41235-7; Sequence=VSP_026030, VSP_003675;
Note=Produced by alternative splicing of isoform HNF4-Alpha-7.;
-!- PTM: Phosphorylated on tyrosine residue(s); phosphorylation is
important for its DNA-binding activity. Phosphorylation may
directly or indirectly play a regulatory role in the subnuclear
distribution. Phosphorylation at Ser-313 by AMPK reduces the
ability to form homodimers and bind DNA.
{ECO:0000269|PubMed:12740371, ECO:0000269|PubMed:21708125,
ECO:0000269|PubMed:7568236}.
-!- PTM: Acetylation at Lys-458 lowers transcriptional activation by
about two-fold. {ECO:0000269|PubMed:21708125}.
-!- DISEASE: Maturity-onset diabetes of the young 1 (MODY1)
[MIM:125850]: 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:10389854,
ECO:0000269|PubMed:17407387, ECO:0000269|PubMed:9243109,
ECO:0000269|PubMed:9313765}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM)
[MIM:125853]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:9449683}.
Note=Disease susceptibility may be associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Fanconi renotubular syndrome 4 with maturity-onset
diabetes of the young (FRTS4) [MIM:616026]: A disease
characterized by Fanconi syndrome associated with a beta cell
phenotype of neonatal hyperinsulinism with macrosomia and young
onset diabetes. Fanconi syndrome is a proximal tubulopathy
resulting in generalised aminoaciduria, low molecular weight
proteinuria, glycosuria, hyperphosphaturia and hypouricemia. Some
FRTS4 patients have nephrocalcinosis, renal impairment,
hypercalciuria with relative hypocalcemia, and hypermagnesemia.
{ECO:0000269|PubMed:22802087, ECO:0000269|PubMed:24285859}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Binds fatty acids.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB48082.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA54248.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA61133.1; Type=Frameshift; Positions=2, 7; Evidence={ECO:0000305};
Sequence=CAA61134.1; Type=Frameshift; Positions=2, 7; Evidence={ECO:0000305};
Sequence=CAA61135.1; Type=Frameshift; Positions=2, 7; Evidence={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/hnf4a/";
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EMBL; X87870; CAA61133.1; ALT_FRAME; mRNA.
EMBL; X87871; CAA61134.1; ALT_FRAME; mRNA.
EMBL; X87872; CAA61135.1; ALT_FRAME; mRNA.
EMBL; Z49825; CAA89989.1; -; mRNA.
EMBL; AY680696; AAT91237.1; -; mRNA.
EMBL; AY680697; AAT91238.1; -; mRNA.
EMBL; AY680698; AAT91239.1; -; mRNA.
EMBL; U72969; AAB48082.1; ALT_SEQ; Genomic_DNA.
EMBL; U72959; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72961; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72962; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72963; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72964; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72965; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72966; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72967; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72968; AAB48082.1; JOINED; Genomic_DNA.
EMBL; U72967; AAB48083.1; -; Genomic_DNA.
EMBL; U72959; AAB48083.1; JOINED; Genomic_DNA.
EMBL; U72961; AAB48083.1; JOINED; Genomic_DNA.
EMBL; U72962; AAB48083.1; JOINED; Genomic_DNA.
EMBL; U72963; AAB48083.1; JOINED; Genomic_DNA.
EMBL; U72964; AAB48083.1; JOINED; Genomic_DNA.
EMBL; U72965; AAB48083.1; JOINED; Genomic_DNA.
EMBL; U72966; AAB48083.1; JOINED; Genomic_DNA.
EMBL; EF591040; ABQ52204.1; -; Genomic_DNA.
EMBL; AL132772; CAC01303.1; -; Genomic_DNA.
EMBL; AL132772; CAI18856.1; -; Genomic_DNA.
EMBL; CH471077; EAW75924.1; -; Genomic_DNA.
EMBL; CH471077; EAW75925.1; -; Genomic_DNA.
EMBL; BC137539; AAI37540.1; -; mRNA.
EMBL; BC137540; AAI37541.1; -; mRNA.
EMBL; X76930; CAA54248.1; ALT_INIT; mRNA.
CCDS; CCDS13330.1; -. [P41235-1]
CCDS; CCDS13331.1; -. [P41235-3]
CCDS; CCDS42876.1; -. [P41235-5]
CCDS; CCDS46604.1; -. [P41235-6]
CCDS; CCDS46605.1; -. [P41235-2]
CCDS; CCDS68131.1; -. [P41235-7]
PIR; JC4937; JC4937.
PIR; JC4938; JC4938.
PIR; JC6096; JC6096.
RefSeq; NP_000448.3; NM_000457.4. [P41235-1]
RefSeq; NP_001025174.1; NM_001030003.2. [P41235-6]
RefSeq; NP_001025175.1; NM_001030004.2. [P41235-7]
RefSeq; NP_001245284.1; NM_001258355.1.
RefSeq; NP_001274111.1; NM_001287182.1.
RefSeq; NP_001274112.1; NM_001287183.1.
RefSeq; NP_001274113.1; NM_001287184.1.
RefSeq; NP_787110.2; NM_175914.4. [P41235-5]
RefSeq; NP_849181.1; NM_178850.2. [P41235-3]
UniGene; Hs.116462; -.
PDB; 1PZL; X-ray; 2.10 A; A=142-378.
PDB; 3CBB; X-ray; 2.00 A; A/B=58-135.
PDB; 3FS1; X-ray; 2.20 A; A=148-377.
PDB; 4B7W; X-ray; 4.00 A; A/B/C/D=142-377.
PDB; 4IQR; X-ray; 2.90 A; A/B/E/F=55-377.
PDBsum; 1PZL; -.
PDBsum; 3CBB; -.
PDBsum; 3FS1; -.
PDBsum; 4B7W; -.
PDBsum; 4IQR; -.
ProteinModelPortal; P41235; -.
SMR; P41235; -.
BioGrid; 109414; 69.
CORUM; P41235; -.
DIP; DIP-499N; -.
IntAct; P41235; 21.
MINT; MINT-269829; -.
STRING; 9606.ENSP00000312987; -.
BindingDB; P41235; -.
ChEMBL; CHEMBL5398; -.
DrugBank; DB05447; AVI-4557.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB08231; MYRISTIC ACID.
iPTMnet; P41235; -.
PhosphoSitePlus; P41235; -.
BioMuta; HNF4A; -.
DMDM; 148886624; -.
MaxQB; P41235; -.
PaxDb; P41235; -.
PeptideAtlas; P41235; -.
PRIDE; P41235; -.
Ensembl; ENST00000316099; ENSP00000312987; ENSG00000101076. [P41235-1]
Ensembl; ENST00000316673; ENSP00000315180; ENSG00000101076. [P41235-5]
Ensembl; ENST00000415691; ENSP00000412111; ENSG00000101076. [P41235-2]
Ensembl; ENST00000443598; ENSP00000410911; ENSG00000101076. [P41235-3]
Ensembl; ENST00000457232; ENSP00000396216; ENSG00000101076. [P41235-6]
Ensembl; ENST00000609795; ENSP00000476609; ENSG00000101076. [P41235-7]
GeneID; 3172; -.
KEGG; hsa:3172; -.
UCSC; uc002xlt.4; human. [P41235-1]
CTD; 3172; -.
DisGeNET; 3172; -.
EuPathDB; HostDB:ENSG00000101076.16; -.
GeneCards; HNF4A; -.
GeneReviews; HNF4A; -.
HGNC; HGNC:5024; HNF4A.
HPA; CAB019417; -.
HPA; HPA004712; -.
MalaCards; HNF4A; -.
MIM; 125850; phenotype.
MIM; 125853; phenotype.
MIM; 600281; gene.
MIM; 606391; phenotype.
MIM; 616026; phenotype.
neXtProt; NX_P41235; -.
OpenTargets; ENSG00000101076; -.
Orphanet; 263455; Hyperinsulinism due to HNF4A deficiency.
Orphanet; 552; MODY.
PharmGKB; PA29349; -.
eggNOG; KOG4215; Eukaryota.
eggNOG; ENOG410XQT8; LUCA.
GeneTree; ENSGT00760000118948; -.
HOVERGEN; HBG005606; -.
InParanoid; P41235; -.
KO; K07292; -.
OMA; KRMRYQV; -.
OrthoDB; EOG091G0A89; -.
PhylomeDB; P41235; -.
TreeFam; TF352097; -.
Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; P41235; -.
SIGNOR; P41235; -.
EvolutionaryTrace; P41235; -.
GeneWiki; Hepatocyte_nuclear_factor_4_alpha; -.
GenomeRNAi; 3172; -.
PRO; PR:P41235; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101076; -.
ExpressionAtlas; P41235; baseline and differential.
Genevisible; P41235; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
GO; GO:0005504; F:fatty acid binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0005102; F:receptor binding; IDA:BHF-UCL.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISS:BHF-UCL.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; IDA:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; ISS:BHF-UCL.
GO; GO:0055088; P:lipid homeostasis; IMP:BHF-UCL.
GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0006591; P:ornithine metabolic process; IMP:BHF-UCL.
GO; GO:0055091; P:phospholipid homeostasis; ISS:BHF-UCL.
GO; GO:2000189; P:positive regulation of cholesterol homeostasis; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0010470; P:regulation of gastrulation; IEA:Ensembl.
GO; GO:0060398; P:regulation of growth hormone receptor signaling pathway; NAS:BHF-UCL.
GO; GO:0050796; P:regulation of insulin secretion; ISS:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; IDA:BHF-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0009749; P:response to glucose; ISS:BHF-UCL.
GO; GO:0007548; P:sex differentiation; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0070328; P:triglyceride homeostasis; ISS:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; IMP:BHF-UCL.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003068; COUP_TF.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01282; COUPTNFACTOR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative promoter usage;
Alternative splicing; Complete proteome; Diabetes mellitus;
Disease mutation; DNA-binding; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 474 Hepatocyte nuclear factor 4-alpha.
/FTId=PRO_0000053558.
DNA_BIND 57 132 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 60 80 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 96 120 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000269|PubMed:21708125}.
MOD_RES 144 144 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 166 166 Phosphothreonine.
{ECO:0000269|PubMed:21708125}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000269|PubMed:21708125}.
MOD_RES 313 313 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:12740371}.
MOD_RES 429 429 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 432 432 Phosphothreonine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:21708125}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:21708125}.
MOD_RES 458 458 N6-acetyllysine.
{ECO:0000269|PubMed:21708125}.
CROSSLNK 234 234 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21708125}.
CROSSLNK 307 307 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21708125}.
VAR_SEQ 1 38 MRLSKTLVDMDMADYSAALDPAYTTLEFENVQVLTMGN ->
MVSVNAPLGAPVESSY (in isoform HNF4-Alpha-
7, isoform HNF4-Alpha-8 and isoform HNF4-
Alpha-9). {ECO:0000305}.
/FTId=VSP_026030.
VAR_SEQ 38 38 N -> NDLLPLRLARLRHPLRHHWSISGGVDSSPQG (in
isoform HNF4-Alpha-4). {ECO:0000305}.
/FTId=VSP_003673.
VAR_SEQ 378 474 SPSDAPHAHHPLHPHLMQEHMGTNVIVANTMPTHLSNGQMC
EWPRPRGQAATPETPQPSPPGGSGSEPYKLLPGAVATIVKP
LSAIPQPTITKQEVI -> PCQAQEGRGWSGDSPGDRPHTV
SSPLSSLASPLCRFGQVA (in isoform HNF4-
Alpha-3 and isoform HNF4-Alpha-9).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8964514}.
/FTId=VSP_003675.
VAR_SEQ 418 428 CEWPRPRGQAA -> S (in isoform HNF4-Alpha-2
and isoform HNF4-Alpha-8).
{ECO:0000303|PubMed:8964514}.
/FTId=VSP_003674.
VARIANT 85 85 R -> W (in FRTS4; dbSNP:rs587777732).
{ECO:0000269|PubMed:22802087,
ECO:0000269|PubMed:24285859}.
/FTId=VAR_071951.
VARIANT 136 136 R -> W (in MODY1; dbSNP:rs137853336).
{ECO:0000269|PubMed:9313765}.
/FTId=VAR_004668.
VARIANT 139 139 T -> I (in dbSNP:rs1800961).
{ECO:0000269|PubMed:9267996,
ECO:0000269|Ref.5}.
/FTId=VAR_004669.
VARIANT 264 264 V -> M (rare polymorphism found in a
patient with non-insulin-dependent
diabetes mellitus; does not affect
activity; dbSNP:rs139779712).
{ECO:0000269|PubMed:10389854,
ECO:0000269|PubMed:9267996}.
/FTId=VAR_010600.
VARIANT 285 285 E -> Q (in MODY1; results in loss of
function). {ECO:0000269|PubMed:10389854,
ECO:0000269|PubMed:9243109}.
/FTId=VAR_010601.
VARIANT 373 373 M -> R (in MODY1; dbSNP:rs137853338).
{ECO:0000269|PubMed:17407387}.
/FTId=VAR_071952.
VARIANT 402 402 V -> I (in NIDDM; reduced transactivation
activity; dbSNP:rs137853337).
{ECO:0000269|PubMed:9449683}.
/FTId=VAR_004670.
VARIANT 445 445 P -> S (in dbSNP:rs1063239).
{ECO:0000269|PubMed:8964514}.
/FTId=VAR_011785.
VARIANT 453 453 V -> I (in dbSNP:rs776824742).
{ECO:0000269|Ref.5}.
/FTId=VAR_062267.
MUTAGEN 313 313 S->A: Abolishes AMPK-mediated
phosphorylation.
{ECO:0000269|PubMed:12740371}.
MUTAGEN 313 313 S->D: Phosphomimetic mutant that leads to
reduced ability to bind DNA.
{ECO:0000269|PubMed:12740371}.
CONFLICT 440 440 G -> A (in Ref. 9; CAA54248).
{ECO:0000305}.
TURN 61 63 {ECO:0000244|PDB:3CBB}.
STRAND 64 66 {ECO:0000244|PDB:3CBB}.
STRAND 69 71 {ECO:0000244|PDB:3CBB}.
HELIX 78 89 {ECO:0000244|PDB:3CBB}.
STRAND 97 100 {ECO:0000244|PDB:4IQR}.
TURN 106 111 {ECO:0000244|PDB:3CBB}.
HELIX 113 123 {ECO:0000244|PDB:3CBB}.
HELIX 127 129 {ECO:0000244|PDB:3CBB}.
HELIX 149 153 {ECO:0000244|PDB:1PZL}.
HELIX 155 163 {ECO:0000244|PDB:1PZL}.
TURN 176 178 {ECO:0000244|PDB:1PZL}.
HELIX 184 202 {ECO:0000244|PDB:1PZL}.
HELIX 206 209 {ECO:0000244|PDB:1PZL}.
HELIX 213 222 {ECO:0000244|PDB:1PZL}.
HELIX 224 236 {ECO:0000244|PDB:1PZL}.
STRAND 239 244 {ECO:0000244|PDB:1PZL}.
STRAND 250 254 {ECO:0000244|PDB:1PZL}.
HELIX 256 261 {ECO:0000244|PDB:1PZL}.
HELIX 262 271 {ECO:0000244|PDB:1PZL}.
HELIX 273 279 {ECO:0000244|PDB:1PZL}.
HELIX 283 294 {ECO:0000244|PDB:1PZL}.
HELIX 305 324 {ECO:0000244|PDB:1PZL}.
STRAND 325 328 {ECO:0000244|PDB:1PZL}.
HELIX 333 338 {ECO:0000244|PDB:1PZL}.
HELIX 340 360 {ECO:0000244|PDB:1PZL}.
HELIX 368 374 {ECO:0000244|PDB:1PZL}.
SEQUENCE 474 AA; 52785 MW; 5F1309B89D95DCAF CRC64;
MRLSKTLVDM DMADYSAALD PAYTTLEFEN VQVLTMGNDT SPSEGTNLNA PNSLGVSALC
AICGDRATGK HYGASSCDGC KGFFRRSVRK NHMYSCRFSR QCVVDKDKRN QCRYCRLKKC
FRAGMKKEAV QNERDRISTR RSSYEDSSLP SINALLQAEV LSRQITSPVS GINGDIRAKK
IASIADVCES MKEQLLVLVE WAKYIPAFCE LPLDDQVALL RAHAGEHLLL GATKRSMVFK
DVLLLGNDYI VPRHCPELAE MSRVSIRILD ELVLPFQELQ IDDNEYAYLK AIIFFDPDAK
GLSDPGKIKR LRSQVQVSLE DYINDRQYDS RGRFGELLLL LPTLQSITWQ MIEQIQFIKL
FGMAKIDNLL QEMLLGGSPS DAPHAHHPLH PHLMQEHMGT NVIVANTMPT HLSNGQMCEW
PRPRGQAATP ETPQPSPPGG SGSEPYKLLP GAVATIVKPL SAIPQPTITK QEVI


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