TFAP2A

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Transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha)
Identifiers
Symbol(s) TFAP2A; AP-2; AP-2alpha; AP2TF; TFAP2
External IDs OMIM: 107580 MGI: 104671 HomoloGene: 2421
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 7020 21418
Ensembl ENSG00000137203 ENSMUSG00000021359
Uniprot P05549 Q3UL09
Refseq NM_001032280 (mRNA)
NP_001027451 (protein)		 NM_011547 (mRNA)
NP_035677 (protein)
Location Chr 6: 10.5 - 10.53 Mb Chr 13: 40.73 - 40.75 Mb
Pubmed search [1] [2]

Transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha), also known as TFAP2A, is a human gene.[1]

AP2-alpha is a 52-kD retinoic acid-inducible and developmentally regulated activator of transcription that binds to a consensus DNA-binding sequence CCCCAGGC in the SV40 and metallothionein (MIM 156350) promoters.[supplied by OMIM][1]

Contents

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: TFAP2A transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha).

[edit] Further reading

  • Murphy JE, Keen JH (1992). "Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia.". J. Biol. Chem. 267 (15): 10850–5. PMID 1587861. 
  • Gaynor RB, Muchardt C, Xia YR, et al. (1991). "Localization of the gene for the DNA-binding protein AP-2 to human chromosome 6p22.3-pter.". Genomics 10 (4): 1100–2. PMID 1916817. 
  • Williams T, Tjian R (1991). "Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins.". Science 251 (4997): 1067–71. PMID 1998122. 
  • Williams T, Tjian R (1991). "Analysis of the DNA-binding and activation properties of the human transcription factor AP-2.". Genes Dev. 5 (4): 670–82. PMID 2010091. 
  • Williams T, Admon A, Lüscher B, Tjian R (1989). "Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements.". Genes Dev. 2 (12A): 1557–69. PMID 3063603. 
  • Bauer R, Imhof A, Pscherer A, et al. (1994). "The genomic structure of the human AP-2 transcription factor.". Nucleic Acids Res. 22 (8): 1413–20. PMID 8190633. 
  • Buettner R, Kannan P, Imhof A, et al. (1993). "An alternatively spliced mRNA from the AP-2 gene encodes a negative regulator of transcriptional activation by AP-2.". Mol. Cell. Biol. 13 (7): 4174–85. PMID 8321221. 
  • Williamson JA, Bosher JM, Skinner A, et al. (1996). "Chromosomal mapping of the human and mouse homologues of two new members of the AP-2 family of transcription factors.". Genomics 35 (1): 262–4. doi:10.1006/geno.1996.0351. PMID 8661133. 
  • Pirozzi G, McConnell SJ, Uveges AJ, et al. (1997). "Identification of novel human WW domain-containing proteins by cloning of ligand targets.". J. Biol. Chem. 272 (23): 14611–6. PMID 9169421. 
  • Batsché E, Muchardt C, Behrens J, et al. (1998). "RB and c-Myc activate expression of the E-cadherin gene in epithelial cells through interaction with transcription factor AP-2.". Mol. Cell. Biol. 18 (7): 3647–58. PMID 9632747. 
  • Mertens PR, Alfonso-Jaume MA, Steinmann K, Lovett DH (1999). "A synergistic interaction of transcription factors AP2 and YB-1 regulates gelatinase A enhancer-dependent transcription.". J. Biol. Chem. 273 (49): 32957–65. PMID 9830047. 
  • García MA, Campillos M, Marina A, et al. (1999). "Transcription factor AP-2 activity is modulated by protein kinase A-mediated phosphorylation.". FEBS Lett. 444 (1): 27–31. PMID 10037142. 
  • Rosenthal JA, Chen H, Slepnev VI, et al. (1999). "The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module.". J. Biol. Chem. 274 (48): 33959–65. PMID 10567358. 
  • Heicklen-Klein A, Ginzburg I (2000). "Tau promoter confers neuronal specificity and binds Sp1 and AP-2.". J. Neurochem. 75 (4): 1408–18. PMID 10987820. 
  • Nyormoi O, Wang Z, Doan D, et al. (2001). "Transcription factor AP-2alpha is preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor alpha-induced apoptosis in breast cancer cells.". Mol. Cell. Biol. 21 (15): 4856–67. doi:10.1128/MCB.21.15.4856-4867.2001. PMID 11438643. 
  • Rao DS, Chang JC, Kumar PD, et al. (2001). "Huntingtin interacting protein 1 Is a clathrin coat binding protein required for differentiation of late spermatogenic progenitors.". Mol. Cell. Biol. 21 (22): 7796–806. doi:10.1128/MCB.21.22.7796-7806.2001. PMID 11604514. 
  • Bragança J, Swingler T, Marques FI, et al. (2002). "Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2.". J. Biol. Chem. 277 (10): 8559–65. doi:10.1074/jbc.M110850200. PMID 11744733. 
  • Mertens PR, Steinmann K, Alfonso-Jaume MA, et al. (2002). "Combinatorial interactions of p53, activating protein-2, and YB-1 with a single enhancer element regulate gelatinase A expression in neoplastic cells.". J. Biol. Chem. 277 (28): 24875–82. doi:10.1074/jbc.M200445200. PMID 11973333. 
  • Eloranta JJ, Hurst HC (2002). "Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo.". J. Biol. Chem. 277 (34): 30798–804. doi:10.1074/jbc.M202780200. PMID 12072434. 
  • Ben-Zimra M, Koler M, Orly J (2003). "Transcription of cholesterol side-chain cleavage cytochrome P450 in the placenta: activating protein-2 assumes the role of steroidogenic factor-1 by binding to an overlapping promoter element.". Mol. Endocrinol. 16 (8): 1864–80. PMID 12145340. 

[edit] External links


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v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH)
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1
(1.3) bHLH-ZIP
MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4
GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)
(2.3) Cys2His2
ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6
(2.5) Alternating composition
AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B
(3) Helix-turn-helix
domains
ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1
(3.2) Paired box
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)
HSF (1, 2, 4)
(3.5) Tryptophan clusters
ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2
(3.6) TEA domain
transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)
(4.2) STAT
STAT (1, 2, 3, 4, 5, 6)
(4.3) p53
(4.4) MADS box
Mef2 (A, B, C, D) • SRF
HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1
(4.10) Cold-shock domain
(4.11) Runt
(0) Other
transcription factors
(0.2) HMGI(Y)
HMGA (1, 2) • HBP1
Rb • RBL1 • RBL2
(0.5) AP-2/EREBP-related factors
Apetala 2 • EREBP • B3
(0.6) Miscellaneous
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD