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Protein

Hepatocyte nuclear factor 3-alpha

Gene

FOXA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Its differential recruitment to chromatin is dependent on distribution of histone H3 methylated at 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the development of multiple endoderm-derived organ systems such as liver, pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles (By similarity). Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription; required for ESR1 binding to the NKX2-1 promoter in breast cancer cells; binds to the RPRM promter and is required for the estrogen-induced repression of RPRM. Involved in regulation of apoptosis by inhibiting the expression of BCL2. Involved in cell cycle regulation by activating expression of CDKN1B, alone or in conjunction with BRCA1. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis.By similarity5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi169 – 26092Fork-headPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  3. sequence-specific DNA binding Source: Ensembl
  4. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: GO_Central
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
  6. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. anatomical structure formation involved in morphogenesis Source: Ensembl
  2. chromatin remodeling Source: UniProtKB
  3. dorsal/ventral neural tube patterning Source: Ensembl
  4. epithelial cell maturation involved in prostate gland development Source: Ensembl
  5. epithelial-mesenchymal signaling involved in prostate gland development Source: Ensembl
  6. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  7. glucose homeostasis Source: Ensembl
  8. hormone metabolic process Source: Ensembl
  9. lung epithelial cell differentiation Source: Ensembl
  10. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  11. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  12. neuron fate specification Source: Ensembl
  13. positive regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
  14. positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  15. positive regulation of mitotic cell cycle Source: UniProtKB
  16. positive regulation of neuron differentiation Source: Ensembl
  17. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  18. positive regulation of smoothened signaling pathway Source: Ensembl
  19. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  20. prostate gland epithelium morphogenesis Source: Ensembl
  21. prostate gland stromal morphogenesis Source: Ensembl
  22. response to estradiol Source: UniProtKB
  23. secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: Ensembl
  24. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP55317.

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatocyte nuclear factor 3-alpha
Short name:
HNF-3-alpha
Short name:
HNF-3A
Alternative name(s):
Forkhead box protein A1
Transcription factor 3A
Short name:
TCF-3A
Gene namesi
Name:FOXA1
Synonyms:HNF3A, TCF3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:5021. FOXA1.

Subcellular locationi

Nucleus PROSITE-ProRule annotation2 Publications

GO - Cellular componenti

  1. microvillus Source: Ensembl
  2. nucleolus Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA201090.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 472472Hepatocyte nuclear factor 3-alphaPRO_0000091792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei223 – 2231PhosphoserineBy similarity
Modified residuei293 – 2931PhosphoserineBy similarity
Modified residuei307 – 3071Phosphoserine1 Publication
Modified residuei331 – 3311Phosphoserine1 Publication
Modified residuei472 – 4721PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP55317.
PaxDbiP55317.
PRIDEiP55317.

PTM databases

PhosphoSiteiP55317.

Expressioni

Tissue specificityi

Highly expressed in prostate and ESR1-positive breast tumors. Overexpressed in esophageal and lung adenocarcinomas.3 Publications

Gene expression databases

BgeeiP55317.
CleanExiHS_FOXA1.
ExpressionAtlasiP55317. baseline and differential.
GenevestigatoriP55317.

Organism-specific databases

HPAiCAB011595.
HPA050505.

Interactioni

Subunit structurei

Binds DNA as a monomer (By similarity). Interacts with FOXA2. Interacts with NKX2-1. Interacts with HDAC7. Interacts with the histone H3-H4 heterodimer. Associates with nucleosomes containing histone H2A. Interacts with AR. Interacts with NR0B2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi109411. 9 interactions.
DIPiDIP-57138N.
IntActiP55317. 7 interactions.
MINTiMINT-2804254.
STRINGi9606.ENSP00000250448.

Structurei

3D structure databases

ProteinModelPortaliP55317.
SMRiP55317. Positions 168-267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00760000118904.
HOGENOMiHOG000231817.
HOVERGENiHBG006621.
InParanoidiP55317.
KOiK09387.
OMAiTMNTYMT.
OrthoDBiEOG7C8GHD.
PhylomeDBiP55317.
TreeFamiTF316127.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR013638. Fork-head_N.
IPR018533. Forkhead_box_C.
IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00250. Fork_head. 1 hit.
PF08430. Fork_head_N. 1 hit.
PF09354. HNF_C. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
PROSITEiPS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55317-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLGTVKMEGH ETSDWNSYYA DTQEAYSSVP VSNMNSGLGS MNSMNTYMTM
60 70 80 90 100
NTMTTSGNMT PASFNMSYAN PGLGAGLSPG AVAGMPGGSA GAMNSMTAAG
110 120 130 140 150
VTAMGTALSP SGMGAMGAQQ AASMNGLGPY AAAMNPCMSP MAYAPSNLGR
160 170 180 190 200
SRAGGGGDAK TFKRSYPHAK PPYSYISLIT MAIQQAPSKM LTLSEIYQWI
210 220 230 240 250
MDLFPYYRQN QQRWQNSIRH SLSFNDCFVK VARSPDKPGK GSYWTLHPDS
260 270 280 290 300
GNMFENGCYL RRQKRFKCEK QPGAGGGGGS GSGGSGAKGG PESRKDPSGA
310 320 330 340 350
SNPSADSPLH RGVHGKTGQL EGAPAPGPAA SPQTLDHSGA TATGGASELK
360 370 380 390 400
TPASSTAPPI SSGPGALASV PASHPAHGLA PHESQLHLKG DPHYSFNHPF
410 420 430 440 450
SINNLMSSSE QQHKLDFKAY EQALQYSPYG STLPASLPLG SASVTTRSPI
460 470
EPSALEPAYY QGVYSRPVLN TS
Length:472
Mass (Da):49,148
Last modified:May 18, 2010 - v2
Checksum:iB2489523459EEB4C
GO
Isoform 2 (identifier: P55317-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Note: No experimental confirmation available.

Show »
Length:439
Mass (Da):45,468
Checksum:i170DF8E54E6FC73C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721G → A.2 Publications
VAR_015183
Natural varianti83 – 831A → T.1 Publication
Corresponds to variant rs7144658 [ dbSNP | Ensembl ].
VAR_013457
Natural varianti87 – 871G → E.
Corresponds to variant rs35220193 [ dbSNP | Ensembl ].
VAR_055835
Natural varianti124 – 1241M → MM.2 Publications
VAR_015184
Natural varianti185 – 1851Q → R.2 Publications
VAR_015185
Natural varianti448 – 4481S → N.1 Publication
Corresponds to variant rs33984772 [ dbSNP | Ensembl ].
VAR_013458

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform 2. 1 PublicationVSP_055094Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39840 mRNA. Translation: AAB06493.1.
AF176112, AF176111 Genomic DNA. Translation: AAD51979.1.
AF303743, AF303742 Genomic DNA. Translation: AAG40847.1.
AK313785 mRNA. Translation: BAG36523.1.
AK316360 mRNA. Translation: BAH14731.1.
AL121790 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65844.1.
BC033890 mRNA. Translation: AAH33890.1.
CCDSiCCDS9665.1. [P55317-1]
PIRiS70357.
RefSeqiNP_004487.2. NM_004496.3. [P55317-1]
UniGeneiHs.163484.

Genome annotation databases

EnsembliENST00000250448; ENSP00000250448; ENSG00000129514. [P55317-1]
GeneIDi3169.
KEGGihsa:3169.
UCSCiuc001wuf.4. human. [P55317-1]

Polymorphism databases

DMDMi296434509.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Hepatocyte nuclear factors entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39840 mRNA. Translation: AAB06493.1.
AF176112, AF176111 Genomic DNA. Translation: AAD51979.1.
AF303743, AF303742 Genomic DNA. Translation: AAG40847.1.
AK313785 mRNA. Translation: BAG36523.1.
AK316360 mRNA. Translation: BAH14731.1.
AL121790 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65844.1.
BC033890 mRNA. Translation: AAH33890.1.
CCDSiCCDS9665.1. [P55317-1]
PIRiS70357.
RefSeqiNP_004487.2. NM_004496.3. [P55317-1]
UniGeneiHs.163484.

3D structure databases

ProteinModelPortaliP55317.
SMRiP55317. Positions 168-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109411. 9 interactions.
DIPiDIP-57138N.
IntActiP55317. 7 interactions.
MINTiMINT-2804254.
STRINGi9606.ENSP00000250448.

PTM databases

PhosphoSiteiP55317.

Polymorphism databases

DMDMi296434509.

Proteomic databases

MaxQBiP55317.
PaxDbiP55317.
PRIDEiP55317.

Protocols and materials databases

DNASUi3169.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250448; ENSP00000250448; ENSG00000129514. [P55317-1]
GeneIDi3169.
KEGGihsa:3169.
UCSCiuc001wuf.4. human. [P55317-1]

Organism-specific databases

CTDi3169.
GeneCardsiGC14M038059.
H-InvDBHIX0011609.
HGNCiHGNC:5021. FOXA1.
HPAiCAB011595.
HPA050505.
MIMi602294. gene.
neXtProtiNX_P55317.
PharmGKBiPA201090.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00760000118904.
HOGENOMiHOG000231817.
HOVERGENiHBG006621.
InParanoidiP55317.
KOiK09387.
OMAiTMNTYMT.
OrthoDBiEOG7C8GHD.
PhylomeDBiP55317.
TreeFamiTF316127.

Enzyme and pathway databases

SignaLinkiP55317.

Miscellaneous databases

ChiTaRSiFOXA1. human.
GeneWikiiFOXA1.
GenomeRNAii3169.
NextBioi12564.
PROiP55317.
SOURCEiSearch...

Gene expression databases

BgeeiP55317.
CleanExiHS_FOXA1.
ExpressionAtlasiP55317. baseline and differential.
GenevestigatoriP55317.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR013638. Fork-head_N.
IPR018533. Forkhead_box_C.
IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00250. Fork_head. 1 hit.
PF08430. Fork_head_N. 1 hit.
PF09354. HNF_C. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
PROSITEiPS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the forkhead transcription factor HNF-3 alpha from a human pulmonary adenocarcinoma cell line."
    Bingle C.D., Gowan S.
    Biochim. Biophys. Acta 1307:17-20(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-72; MET-124 INS AND ARG-185.
    Tissue: Lung.
  2. "The human HNF-3 genes: cloning, partial sequence and mutation screening in patients with impaired glucose homeostasis."
    Navas M.A., Vaisse C., Boger S., Heimesaat M., Kollee L.A., Stoffel M.
    Hum. Hered. 50:370-381(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-72; THR-83; MET-124 INS; ARG-185 AND ASN-448.
  3. "Genetic variation in the HNF-3alpha gene."
    Yu L., Takeda J.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Mammary gland and Trachea.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  8. "The hepatocyte nuclear factor 3 alpha gene, HNF3alpha (FOXA1), on chromosome band 14q13 is amplified and overexpressed in esophageal and lung adenocarcinomas."
    Lin L., Miller C.T., Contreras J.I., Prescott M.S., Dagenais S.L., Wu R., Yee J., Orringer M.B., Misek D.E., Hanash S.M., Glover T.W., Beer D.G.
    Cancer Res. 62:5273-5279(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Forkhead box A1 regulates prostate ductal morphogenesis and promotes epithelial cell maturation."
    Gao N., Ishii K., Mirosevich J., Kuwajima S., Oppenheimer S.R., Roberts R.L., Jiang M., Yu X., Shappell S.B., Caprioli R.M., Stoffel M., Hayward S.W., Matusik R.J.
    Development 132:3431-3443(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  10. "Location analysis of estrogen receptor alpha target promoters reveals that FOXA1 defines a domain of the estrogen response."
    Laganiere J., Deblois G., Lefebvre C., Bataille A.R., Robert F., Giguere V.
    Proc. Natl. Acad. Sci. U.S.A. 102:11651-11656(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "BRCA1 and FOXA1 proteins coregulate the expression of the cell cycle-dependent kinase inhibitor p27(Kip1)."
    Williamson E.A., Wolf I., O'Kelly J., Bose S., Tanosaki S., Koeffler H.P.
    Oncogene 25:1391-1399(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "Physical and functional interactions between homeodomain NKX2.1 and winged helix/forkhead FOXA1 in lung epithelial cells."
    Minoo P., Hu L., Xing Y., Zhu N.L., Chen H., Li M., Borok Z., Li C.
    Mol. Cell. Biol. 27:2155-2165(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKX2-1.
  13. "FoxA1 translates epigenetic signatures into enhancer-driven lineage-specific transcription."
    Lupien M., Eeckhoute J., Meyer C.A., Wang Q., Zhang Y., Li W., Carroll J.S., Liu X.S., Brown M.
    Cell 132:958-970(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL TYPE-SPECIFIC TRANSCRIPTION, DIFFERENTIAL RECRUITMENT TO CHROMATIN.
  14. "Role of Foxa1 in regulation of bcl2 expression during oxidative-stress-induced apoptosis in A549 type II pneumocytes."
    Song L., Wei X., Zhang B., Luo X., Liu J., Feng Y., Xiao X.
    Cell Stress Chaperones 14:417-425(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF APOPTOSIS.
  15. "Differential binding and co-binding pattern of FOXA1 and FOXA3 and their relation to H3K4me3 in HepG2 cells revealed by ChIP-seq."
    Motallebipour M., Ameur A., Reddy Bysani M.S., Patra K., Wallerman O., Mangion J., Barker M.A., McKernan K.J., Komorowski J., Wadelius C.
    Genome Biol. 10:R129.0-R129.0(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXA2.
  16. "Histone deacetylase 7 and FoxA1 in estrogen-mediated repression of RPRM."
    Malik S., Jiang S., Garee J.P., Verdin E., Lee A.V., O'Malley B.W., Zhang M., Belaguli N.S., Oesterreich S.
    Mol. Cell. Biol. 30:399-412(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ESR1-MEDIATED TRANSCRIPTION REPRESSION, DIFFERENTIAL RECRUITMENT TO CHROMATIN, INTERACTION WITH HDAC7.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiFOXA1_HUMAN
AccessioniPrimary (citable) accession number: P55317
Secondary accession number(s): B2R9H6, B7ZAP5, Q9H2A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 18, 2010
Last modified: March 4, 2015
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.