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Q9Y261

- FOXA2_HUMAN

UniProt

Q9Y261 - FOXA2_HUMAN

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Protein

Hepatocyte nuclear factor 3-beta

Gene

FOXA2

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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). In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in part redundant roles. 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; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. Involved in regulation of fat metabolism. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi159 – 25294Fork-headPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. adult locomotory behavior Source: ParkinsonsUK-UCL
  2. cell development Source: Ensembl
  3. cell differentiation in hindbrain Source: Ensembl
  4. cell fate specification Source: ParkinsonsUK-UCL
  5. chromatin modification Source: UniProtKB-KW
  6. connective tissue development Source: Ensembl
  7. dopaminergic neuron differentiation Source: ParkinsonsUK-UCL
  8. dorsal/ventral neural tube patterning Source: Ensembl
  9. ectoderm formation Source: Ensembl
  10. endocrine pancreas development Source: BHF-UCL
  11. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  12. in utero embryonic development Source: Ensembl
  13. lung epithelial cell differentiation Source: Ensembl
  14. negative regulation of detection of glucose Source: BHF-UCL
  15. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  16. negative regulation of glucokinase activity Source: BHF-UCL
  17. negative regulation of neuron differentiation Source: Ensembl
  18. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  19. negative regulation of transcription from RNA polymerase II promoter by glucose Source: BHF-UCL
  20. neuron fate specification Source: Ensembl
  21. positive regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
  22. positive regulation of embryonic development Source: UniProtKB
  23. positive regulation of gastrulation Source: UniProtKB
  24. positive regulation of neuron differentiation Source: Ensembl
  25. positive regulation of smoothened signaling pathway Source: Ensembl
  26. positive regulation of transcription, DNA-templated Source: UniProtKB
  27. positive regulation of transcription from RNA polymerase III promoter Source: Ensembl
  28. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  29. positive regulation of transcription from RNA polymerase II promoter by glucose Source: BHF-UCL
  30. primitive streak formation Source: UniProtKB
  31. regulation of blood coagulation Source: UniProtKB
  32. regulation of insulin secretion involved in cellular response to glucose stimulus Source: BHF-UCL
  33. regulation of steroid metabolic process Source: Ensembl
  34. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  35. regulation of transcription from RNA polymerase II promoter involved in detection of glucose Source: BHF-UCL
  36. response to interleukin-6 Source: UniProtKB
  37. signal transduction involved in regulation of gene expression Source: Ensembl
  38. somite rostral/caudal axis specification Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_13819. Regulation of gene expression in beta cells.
SignaLinkiQ9Y261.

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatocyte nuclear factor 3-beta
Short name:
HNF-3-beta
Short name:
HNF-3B
Alternative name(s):
Forkhead box protein A2
Transcription factor 3B
Short name:
TCF-3B
Gene namesi
Name:FOXA2
Synonyms:HNF3B, TCF3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:5022. FOXA2.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation. Cytoplasm 1 Publication
Note: Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner; in response to insulin signaling via AKT1 is exported from the nucleus.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA201091.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Hepatocyte nuclear factor 3-betaPRO_0000091795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561PhosphothreonineBy similarity
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity
Modified residuei303 – 3031PhosphoserineBy similarity
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei309 – 3091PhosphoserineBy similarity
Modified residuei436 – 4361PhosphoserineBy similarity
Modified residuei457 – 4571PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation on Thr-156 abolishes binding to target promoters and subsequent transcription activation upon insulin stimulation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y261.
PaxDbiQ9Y261.
PRIDEiQ9Y261.

PTM databases

PhosphoSiteiQ9Y261.

Expressioni

Gene expression databases

BgeeiQ9Y261.
CleanExiHS_FOXA2.
ExpressionAtlasiQ9Y261. baseline and differential.
GenevestigatoriQ9Y261.

Organism-specific databases

HPAiCAB001388.

Interactioni

Subunit structurei

Binds DNA as a monomer. Binds TLE1 (By similarity). Interacts with FOXA1 and FOXA3. Interacts with PRKDC.By similarity2 Publications

Protein-protein interaction databases

BioGridi109412. 10 interactions.
IntActiQ9Y261. 1 interaction.
MINTiMINT-6610868.
STRINGi9606.ENSP00000315955.

Structurei

3D structure databases

ProteinModelPortaliQ9Y261.
SMRiQ9Y261. Positions 157-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 9380Transactivation domain 1By similarityAdd
BLAST
Regioni361 – 45797Transactivation domain 2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi106 – 1138Nuclear localization signalBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00760000118904.
HOGENOMiHOG000231817.
HOVERGENiHBG006621.
InParanoidiQ9Y261.
KOiK08035.
OMAiTYEQVMH.
OrthoDBiEOG7C8GHD.
PhylomeDBiQ9Y261.
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. Align

Isoform 1 (identifier: Q9Y261-1) [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
MLGAVKMEGH EPSDWSSYYA EPEGYSSVSN MNAGLGMNGM NTYMSMSAAA 
        60         70         80         90        100
MGSGSGNMSA GSMNMSSYVG AGMSPSLAGM SPGAGAMAGM GGSAGAAGVA 
       110        120        130        140        150
GMGPHLSPSL SPLGGQAAGA MGGLAPYANM NSMSPMYGQA GLSRARDPKT 
       160        170        180        190        200
YRRSYTHAKP PYSYISLITM AIQQSPNKML TLSEIYQWIM DLFPFYRQNQ 
       210        220        230        240        250
QRWQNSIRHS LSFNDCFLKV PRSPDKPGKG SFWTLHPDSG NMFENGCYLR 
       260        270        280        290        300
RQKRFKCEKQ LALKEAAGAA GSGKKAAAGA QASQAQLGEA AGPASETPAG 
       310        320        330        340        350
TESPHSSASP CQEHKRGGLG ELKGTPAAAL SPPEPAPSPG QQQQAAAHLL 
       360        370        380        390        400
GPPHHPGLPP EAHLKPEHHY AFNHPFSINN LMSSEQQHHH SHHHHQPHKM 
       410        420        430        440        450
DLKAYEQVMH YPGYGSPMPG SLAMGPVTNK TGLDASPLAA DTSYYQGVYS 

RPIMNSS
Length:457
Mass (Da):48,306
Last modified:November 1, 1999 - v1
Checksum:i61DDE4C75C70680A
GO
Isoform 2 (identifier: Q9Y261-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHSASSM

Show »
Length:463
Mass (Da):48,907
Checksum:i726495A18CAE1677
GO

Sequence cautioni

The sequence AAH11780.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti328 – 3281A → V in Japanese subjects with maturity-onset diabetes of the young; pathological significance unknown. 1 Publication
Corresponds to variant rs199796119 [ dbSNP | Ensembl ].		VAR_008858

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MHSASSM in isoform 2. 1 PublicationVSP_041212

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028021 mRNA. Translation: BAA78106.1.
AF147787 Genomic DNA. Translation: AAD41081.1.
AF176110 Genomic DNA. Translation: AAD51978.1.
AL121722 Genomic DNA. Translation: CAB89773.1.
BC006545 mRNA. Translation: AAH06545.2.
BC011780 mRNA. Translation: AAH11780.1. Different initiation.
BC019288 mRNA. Translation: AAH19288.1.
CCDSiCCDS13147.1. [Q9Y261-1]
CCDS46585.1. [Q9Y261-2]
RefSeqiNP_068556.2. NM_021784.4. [Q9Y261-2]
NP_710141.1. NM_153675.2. [Q9Y261-1]
XP_006723625.1. XM_006723562.1. [Q9Y261-1]
UniGeneiHs.155651.

Genome annotation databases

EnsembliENST00000377115; ENSP00000366319; ENSG00000125798. [Q9Y261-1]
ENST00000419308; ENSP00000400341; ENSG00000125798. [Q9Y261-2]
GeneIDi3170.
KEGGihsa:3170.
UCSCiuc002wsn.3. human. [Q9Y261-1]

Polymorphism databases

DMDMi8134491.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Hepatocyte nuclear factors entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AB028021 mRNA. Translation: BAA78106.1 .
AF147787 Genomic DNA. Translation: AAD41081.1 .
AF176110 Genomic DNA. Translation: AAD51978.1 .
AL121722 Genomic DNA. Translation: CAB89773.1 .
BC006545 mRNA. Translation: AAH06545.2 .
BC011780 mRNA. Translation: AAH11780.1 . Different initiation.
BC019288 mRNA. Translation: AAH19288.1 .
CCDSi CCDS13147.1. [Q9Y261-1 ]
CCDS46585.1. [Q9Y261-2 ]
RefSeqi NP_068556.2. NM_021784.4. [Q9Y261-2 ]
NP_710141.1. NM_153675.2. [Q9Y261-1 ]
XP_006723625.1. XM_006723562.1. [Q9Y261-1 ]
UniGenei Hs.155651.

3D structure databases

ProteinModelPortali Q9Y261.
SMRi Q9Y261. Positions 157-256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109412. 10 interactions.
IntActi Q9Y261. 1 interaction.
MINTi MINT-6610868.
STRINGi 9606.ENSP00000315955.

PTM databases

PhosphoSitei Q9Y261.

Polymorphism databases

DMDMi 8134491.

Proteomic databases

MaxQBi Q9Y261.
PaxDbi Q9Y261.
PRIDEi Q9Y261.

Protocols and materials databases

DNASUi 3170.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377115 ; ENSP00000366319 ; ENSG00000125798 . [Q9Y261-1 ]
ENST00000419308 ; ENSP00000400341 ; ENSG00000125798 . [Q9Y261-2 ]
GeneIDi 3170.
KEGGi hsa:3170.
UCSCi uc002wsn.3. human. [Q9Y261-1 ]

Organism-specific databases

CTDi 3170.
GeneCardsi GC20M022561.
HGNCi HGNC:5022. FOXA2.
HPAi CAB001388.
MIMi 600288. gene.
neXtProti NX_Q9Y261.
PharmGKBi PA201091.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5025.
GeneTreei ENSGT00760000118904.
HOGENOMi HOG000231817.
HOVERGENi HBG006621.
InParanoidi Q9Y261.
KOi K08035.
OMAi TYEQVMH.
OrthoDBi EOG7C8GHD.
PhylomeDBi Q9Y261.
TreeFami TF316127.

Enzyme and pathway databases

Reactomei REACT_13819. Regulation of gene expression in beta cells.
SignaLinki Q9Y261.

Miscellaneous databases

ChiTaRSi FOXA2. human.
GeneWikii FOXA2.
GenomeRNAii 3170.
NextBioi 12568.
PROi Q9Y261.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y261.
CleanExi HS_FOXA2.
ExpressionAtlasi Q9Y261. baseline and differential.
Genevestigatori Q9Y261.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR013638. Fork-head_N.
IPR018533. Forkhead_box_C.
IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00250. Fork_head. 1 hit.
PF08430. Fork_head_N. 1 hit.
PF09354. HNF_C. 1 hit.
[Graphical view ]
PRINTSi PR00053. FORKHEAD.
SMARTi SM00339. FH. 1 hit.
[Graphical view ]
PROSITEi PS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNA and the gene encoding human hepatocyte nuclear factor (HNF)-3 beta and mutation screening in Japanese subjects with maturity-onset diabetes of the young."
    Yamada S., Zhu Q., Aihara Y., Onda H., Zhang Z., Yu L., Jin L., Si Y.J., Nishigori H., Tomura H., Inoue I., Morikawa A., Yamagata K., Hanafusa T., Matsuzawa Y., Takeda J.
    Diabetologia 43:121-124(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT VAL-328.
    Tissue: Liver.
  2. "No evidence for diabetes-associated mutations in the hepatocyte nuclear factor-3 beta gene in Japanese patients with MODY."
    Hinokio Y., Horikawa Y., Furuta H., Cox N.J., Iwasaki N., Honda M., Ogata M., Iwamoto Y., Bell G.I.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Lung.
  6. "Insulin regulates the activity of forkhead transcription factor Hnf-3beta/Foxa-2 by Akt-mediated phosphorylation and nuclear/cytosolic localization."
    Wolfrum C., Besser D., Luca E., Stoffel M.
    Proc. Natl. Acad. Sci. U.S.A. 100:11624-11629(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "A hepatocyte nuclear factor-3 site in the fibrinogen beta promoter is important for interleukin 6-induced expression, and its activity is influenced by the adjacent -148C/T polymorphism."
    Verschuur M., de Jong M., Felida L., de Maat M.P., Vos H.L.
    J. Biol. Chem. 280:16763-16771(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROMOTER-BINDING.
  8. "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 FOXA1 AND FOXA3.
  9. "Identification of DNA-dependent protein kinase as a cofactor for the forkhead transcription factor FoxA2."
    Nock A., Ascano J.M., Jones T., Barrero M.J., Sugiyama N., Tomita M., Ishihama Y., Malik S.
    J. Biol. Chem. 284:19915-19926(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKDC.
+Additional computationally mapped references.

Entry informationi

Entry nameiFOXA2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y261
Secondary accession number(s): Q8WUW4, Q96DF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 7, 2015
This is version 147 of the entry and version 1 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 20
    Human chromosome 20: 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.
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