AP2A_HUMAN
ID AP2A_HUMAN Reviewed; 437 AA.
AC P05549; Q13777; Q5TAV5; Q8N1C6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Transcription factor AP-2-alpha;
DE Short=AP2-alpha;
DE AltName: Full=AP-2 transcription factor;
DE AltName: Full=Activating enhancer-binding protein 2-alpha;
DE AltName: Full=Activator protein 2;
DE Short=AP-2;
GN Name=TFAP2A; Synonyms=AP2TF, TFAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3063603; DOI=10.1101/gad.2.12a.1557;
RA Williams T., Admon A., Luescher B., Tjian R.;
RT "Cloning and expression of AP-2, a cell-type-specific transcription factor
RT that activates inducible enhancer elements.";
RL Genes Dev. 2:1557-1569(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Teratocarcinoma;
RX PubMed=8321221; DOI=10.1128/mcb.13.7.4174-4185.1993;
RA Buettner R., Kannan P., Imhof A., Bauer R., Yim S.O., Glockshuber R.,
RA Van Dyke M.W., Tainsky M.A.;
RT "An alternatively spliced mRNA from the AP-2 gene encodes a negative
RT regulator of transcriptional activation by AP-2.";
RL Mol. Cell. Biol. 13:4174-4185(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8190633; DOI=10.1093/nar/22.8.1413;
RA Bauer R., Imhof A., Pscherer A., Kopp H., Moser M., Seegers S.,
RA Kerscher M., Tainsky M.A., Hofstaedter F., Buettner R.;
RT "The genomic structure of the human AP-2 transcription factor.";
RL Nucleic Acids Res. 22:1413-1420(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBUNIT.
RX PubMed=1998122; DOI=10.1126/science.1998122;
RA Williams T., Tjian R.;
RT "Characterization of a dimerization motif in AP-2 and its function in
RT heterologous DNA-binding proteins.";
RL Science 251:1067-1071(1991).
RN [8]
RP DNA-BINDING.
RX PubMed=2010091; DOI=10.1101/gad.5.4.670;
RA Williams T., Tjian R.;
RT "Analysis of the DNA-binding and activation properties of the human
RT transcription factor AP-2.";
RL Genes Dev. 5:670-682(1991).
RN [9]
RP PHOSPHORYLATION AT SER-239, AND MUTAGENESIS OF SER-239.
RX PubMed=10037142; DOI=10.1016/s0014-5793(99)00021-6;
RA Garcia M.A., Campillos M., Marina A., Valdivieso F., Vazquez J.;
RT "Transcription factor AP-2 activity is modulated by protein kinase A-
RT mediated phosphorylation.";
RL FEBS Lett. 444:27-31(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH CITED2.
RX PubMed=11694877; DOI=10.1038/ng768;
RA Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I.,
RA Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.;
RT "Cardiac malformations, adrenal agenesis, neural crest defects and
RT exencephaly in mice lacking Cited2, a new Tfap2 co-activator.";
RL Nat. Genet. 29:469-474(2001).
RN [11]
RP INTERACTION WITH CITED4.
RX PubMed=11744733; DOI=10.1074/jbc.m110850200;
RA Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J.,
RA Hurst H.C., Shioda T., Bhattacharya S.;
RT "Human CREB-binding protein/p300-interacting transactivator with ED-rich
RT tail (CITED) 4, a new member of the CITED family, functions as a co-
RT activator for transcription factor AP-2.";
RL J. Biol. Chem. 277:8559-8565(2002).
RN [12]
RP INTERACTION WITH UBE2I, AND SUMOYLATION AT LYS-10.
RX PubMed=12072434; DOI=10.1074/jbc.m202780200;
RA Eloranta J.J., Hurst H.C.;
RT "Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9
RT and is sumolated in vivo.";
RL J. Biol. Chem. 277:30798-30804(2002).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND INTERACTION WITH CITED2
RP AND EP300.
RX PubMed=12586840; DOI=10.1074/jbc.m208144200;
RA Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C.,
RA Bhattacharya S.;
RT "Physical and functional interactions among AP-2 transcription factors,
RT p300/CREB-binding protein, and CITED2.";
RL J. Biol. Chem. 278:16021-16029(2003).
RN [14]
RP INTERACTION WITH RALBP1.
RX PubMed=12775724; DOI=10.1074/jbc.m302191200;
RA Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
RT "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
RT phosphorylate epsin during the switch off of endocytosis in mitosis.";
RL J. Biol. Chem. 278:30597-30604(2003).
RN [15]
RP INTERACTION WITH WWOX, AND DOMAIN.
RX PubMed=15548692; DOI=10.1158/0008-5472.can-04-2055;
RA Aqeilan R.I., Palamarchuk A., Weigel R.J., Herrero J.J., Pekarsky Y.,
RA Croce C.M.;
RT "Physical and functional interactions between the Wwox tumor suppressor
RT protein and the AP-2gamma transcription factor.";
RL Cancer Res. 64:8256-8261(2004).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP INTERACTION WITH KCTD1.
RX PubMed=19115315; DOI=10.1002/jcb.22002;
RA Ding X., Luo C., Zhou J., Zhong Y., Hu X., Zhou F., Ren K., Gan L., He A.,
RA Zhu J., Gao X., Zhang J.;
RT "The interaction of KCTD1 with transcription factor AP-2alpha inhibits its
RT transactivation.";
RL J. Cell. Biochem. 106:285-295(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP INTERACTION WITH KCTD15.
RX PubMed=23382213; DOI=10.1073/pnas.1300203110;
RA Zarelli V.E., Dawid I.B.;
RT "Inhibition of neural crest formation by Kctd15 involves regulation of
RT transcription factor AP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2870-2875(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-177 AND LYS-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP VARIANTS BOFS PRO-249; GLY-254; GLY-255 AND GLU-262.
RX PubMed=18423521; DOI=10.1016/j.ajhg.2008.03.005;
RA Milunsky J.M., Maher T.A., Zhao G., Roberts A.E., Stalker H.J., Zori R.T.,
RA Burch M.N., Clemens M., Mulliken J.B., Smith R., Lin A.E.;
RT "TFAP2A mutations result in branchio-oculo-facial syndrome.";
RL Am. J. Hum. Genet. 82:1171-1177(2008).
CC -!- FUNCTION: Sequence-specific DNA-binding protein that interacts with
CC inducible viral and cellular enhancer elements to regulate
CC transcription of selected genes. AP-2 factors bind to the consensus
CC sequence 5'-GCCNNNGGC-3' and activate genes involved in a large
CC spectrum of important biological functions including proper eye, face,
CC body wall, limb and neural tube development. They also suppress a
CC number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha
CC is the only AP-2 protein required for early morphogenesis of the lens
CC vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1
CC promoter transcription activation. Associates with chromatin to the
CC PITX2 P1 promoter region. {ECO:0000269|PubMed:11694877,
CC ECO:0000269|PubMed:12586840}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members. Interacts with WWOX. Interacts with CITED4.
CC Interacts with UBE2I. Interacts with RALBP1 in a complex also
CC containing EPN1 and NUMB during interphase and mitosis. Interacts with
CC KCTD1; this interaction represses transcription activation. Interacts
CC (via C-terminus) with CITED2 (via C-terminus); the interaction
CC stimulates TFAP2A-transcriptional activation. Interacts (via N-
CC terminus) with EP300 (via N-terminus); the interaction requires CITED2.
CC Interacts with KCTD15; this interaction inhibits TFAP2A transcriptional
CC activation. {ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:11744733,
CC ECO:0000269|PubMed:12072434, ECO:0000269|PubMed:12586840,
CC ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:15548692,
CC ECO:0000269|PubMed:19115315, ECO:0000269|PubMed:1998122,
CC ECO:0000269|PubMed:23382213}.
CC -!- INTERACTION:
CC P05549; Q09472: EP300; NbExp=7; IntAct=EBI-347351, EBI-447295;
CC P05549; Q9H4Y5: GSTO2; NbExp=4; IntAct=EBI-347351, EBI-10194609;
CC P05549; P61244: MAX; NbExp=2; IntAct=EBI-347351, EBI-751711;
CC P05549; Q13064: MKRN3; NbExp=3; IntAct=EBI-347351, EBI-2340269;
CC P05549; P06748: NPM1; NbExp=6; IntAct=EBI-347351, EBI-78579;
CC P05549; P63279: UBE2I; NbExp=4; IntAct=EBI-347351, EBI-80168;
CC P05549-5; Q9H4Y5: GSTO2; NbExp=6; IntAct=EBI-12194905, EBI-10194609;
CC P05549-5; Q0VD86: INCA1; NbExp=3; IntAct=EBI-12194905, EBI-6509505;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12586840}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=AP-2A;
CC IsoId=P05549-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05549-5; Sequence=VSP_043268;
CC Name=4; Synonyms=AP-2B;
CC IsoId=P05549-2; Sequence=VSP_006401;
CC Name=5;
CC IsoId=P05549-6; Sequence=VSP_047050;
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250}.
CC -!- PTM: Sumoylated on Lys-10; which inhibits transcriptional activity.
CC {ECO:0000305|PubMed:12072434}.
CC -!- DISEASE: Branchiooculofacial syndrome (BOFS) [MIM:113620]: A syndrome
CC characterized by growth retardation, bilateral branchial sinus defects
CC with hemangiomatous, scarred skin, cleft lip with or without cleft
CC palate, pseudocleft of the upper lip, nasolacrimal duct obstruction,
CC low set ears with posterior rotation, a malformed, asymmetrical nose
CC with a broad bridge and flattened tip, conductive or sensorineural
CC deafness, ocular and renal anomalies. {ECO:0000269|PubMed:18423521}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: May be an aberrantly processed form with no
CC significant distribution in vivo. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Activating protein 2 entry;
CC URL="https://en.wikipedia.org/wiki/Activating_protein_2";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TFAP2AID42526ch6p24.html";
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DR EMBL; M36711; AAA35539.1; -; mRNA.
DR EMBL; M61156; AAA02487.1; -; mRNA.
DR EMBL; X52611; CAA36842.1; -; mRNA.
DR EMBL; X77343; CAB59735.1; -; Genomic_DNA.
DR EMBL; AL138885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55249.1; -; Genomic_DNA.
DR EMBL; BC017754; AAH17754.1; -; mRNA.
DR CCDS; CCDS34337.1; -. [P05549-5]
DR CCDS; CCDS43422.1; -. [P05549-6]
DR PIR; A31752; A31752.
DR RefSeq; NP_001027451.1; NM_001032280.2. [P05549-5]
DR RefSeq; NP_001035890.1; NM_001042425.1. [P05549-6]
DR RefSeq; NP_003211.1; NM_003220.2.
DR AlphaFoldDB; P05549; -.
DR BioGRID; 112878; 94.
DR CORUM; P05549; -.
DR IntAct; P05549; 104.
DR MINT; P05549; -.
DR STRING; 9606.ENSP00000368924; -.
DR iPTMnet; P05549; -.
DR PhosphoSitePlus; P05549; -.
DR BioMuta; TFAP2A; -.
DR DMDM; 135302; -.
DR EPD; P05549; -.
DR jPOST; P05549; -.
DR MassIVE; P05549; -.
DR MaxQB; P05549; -.
DR PaxDb; P05549; -.
DR PeptideAtlas; P05549; -.
DR PRIDE; P05549; -.
DR ProteomicsDB; 51847; -. [P05549-1]
DR ProteomicsDB; 51848; -. [P05549-2]
DR ProteomicsDB; 51849; -. [P05549-5]
DR ProteomicsDB; 64874; -.
DR Antibodypedia; 3770; 551 antibodies from 37 providers.
DR DNASU; 7020; -.
DR Ensembl; ENST00000319516.8; ENSP00000316516.4; ENSG00000137203.15. [P05549-6]
DR Ensembl; ENST00000379608.9; ENSP00000368928.3; ENSG00000137203.15. [P05549-5]
DR GeneID; 7020; -.
DR KEGG; hsa:7020; -.
DR UCSC; uc003myq.4; human. [P05549-1]
DR CTD; 7020; -.
DR DisGeNET; 7020; -.
DR GeneCards; TFAP2A; -.
DR GeneReviews; TFAP2A; -.
DR HGNC; HGNC:11742; TFAP2A.
DR HPA; ENSG00000137203; Tissue enhanced (breast, skin).
DR MalaCards; TFAP2A; -.
DR MIM; 107580; gene.
DR MIM; 113620; phenotype.
DR neXtProt; NX_P05549; -.
DR OpenTargets; ENSG00000137203; -.
DR Orphanet; 1297; Branchio-oculo-facial syndrome.
DR PharmGKB; PA36459; -.
DR VEuPathDB; HostDB:ENSG00000137203; -.
DR eggNOG; KOG3811; Eukaryota.
DR GeneTree; ENSGT00950000182848; -.
DR HOGENOM; CLU_035175_4_1_1; -.
DR InParanoid; P05549; -.
DR OrthoDB; 641707at2759; -.
DR PhylomeDB; P05549; -.
DR TreeFam; TF313718; -.
DR PathwayCommons; P05549; -.
DR Reactome; R-HSA-3232118; SUMOylation of transcription factors. [P05549-1]
DR Reactome; R-HSA-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
DR Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-HSA-8866906; TFAP2 (AP-2) family regulates transcription of other transcription factors.
DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR Reactome; R-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR SignaLink; P05549; -.
DR SIGNOR; P05549; -.
DR BioGRID-ORCS; 7020; 45 hits in 1098 CRISPR screens.
DR ChiTaRS; TFAP2A; human.
DR GeneWiki; TFAP2A; -.
DR GenomeRNAi; 7020; -.
DR Pharos; P05549; Tbio.
DR PRO; PR:P05549; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P05549; protein.
DR Bgee; ENSG00000137203; Expressed in upper leg skin and 156 other tissues.
DR ExpressionAtlas; P05549; baseline and differential.
DR Genevisible; P05549; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0140536; F:nuclear receptor corepressor activity; IMP:ARUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0071281; P:cellular response to iron ion; IDA:UniProtKB.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; ISS:UniProtKB.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0021623; P:oculomotor nerve formation; ISS:UniProtKB.
DR GO; GO:0003409; P:optic cup structural organization; ISS:UniProtKB.
DR GO; GO:0003404; P:optic vesicle morphogenesis; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0070172; P:positive regulation of tooth mineralization; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010842; P:retina layer formation; IEP:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0021559; P:trigeminal nerve development; ISS:UniProtKB.
DR InterPro; IPR004979; TF_AP2.
DR InterPro; IPR008121; TF_AP2_alpha_N.
DR InterPro; IPR013854; TF_AP2_C.
DR PANTHER; PTHR10812; PTHR10812; 1.
DR Pfam; PF03299; TF_AP-2; 1.
DR PRINTS; PR01749; AP2ATNSCPFCT.
DR PRINTS; PR01748; AP2TNSCPFCT.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Direct protein sequencing;
KW Disease variant; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..437
FT /note="Transcription factor AP-2-alpha"
FT /id="PRO_0000184796"
FT REGION 14..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..410
FT /note="H-S-H (helix-span-helix), dimerization"
FT /evidence="ECO:0000269|PubMed:1998122"
FT REGION 414..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..62
FT /note="PPxY motif"
FT COMPBIAS 23..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:10037142"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:12072434"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..15
FT /note="MLWKLTDNIKYEDCE -> MLVHSFSAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043268"
FT VAR_SEQ 1..15
FT /note="MLWKLTDNIKYEDCE -> MSILAKMGDWQ (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047050"
FT VAR_SEQ 296..437
FT /note="EAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKE
FT FTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEAL
FT KAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK -> KRIHLLTRRNFLLGKWIIFSGQMF
FT GRILCQLGSFIFAENIARCEWNYFMAKRNICMYSYTSILLPSFPLP (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:8321221"
FT /id="VSP_006401"
FT VARIANT 249
FT /note="L -> P (in BOFS)"
FT /evidence="ECO:0000269|PubMed:18423521"
FT /id="VAR_045838"
FT VARIANT 254
FT /note="R -> G (in BOFS; dbSNP:rs151344528)"
FT /evidence="ECO:0000269|PubMed:18423521"
FT /id="VAR_045839"
FT VARIANT 255
FT /note="R -> G (in BOFS; dbSNP:rs121909574)"
FT /evidence="ECO:0000269|PubMed:18423521"
FT /id="VAR_045840"
FT VARIANT 262
FT /note="G -> E (in BOFS; dbSNP:rs121909575)"
FT /evidence="ECO:0000269|PubMed:18423521"
FT /id="VAR_045841"
FT MUTAGEN 239
FT /note="S->A: No phosphorylation."
FT /evidence="ECO:0000269|PubMed:10037142"
SQ SEQUENCE 437 AA; 48062 MW; FB8FA33C3AEED71F CRC64;
MLWKLTDNIK YEDCEDRHDG TSNGTARLPQ LGTVGQSPYT SAPPLSHTPN ADFQPPYFPP
PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR QSQESGLLHT HRGLPHQLSG
LDPRRDYRRH EDLLHGPHAL SSGLGDLSIH SLPHAIEEVP HVEDPGINIP DQTVIKKGPV
SLSKSNSNAV SAIPINKDNL FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP
PECLNASLLG GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGEAVHL
ARDFGYVCET EFPAKAVAEF LNRQHSDPNE QVTRKNMLLA TKQICKEFTD LLAQDRSPLG
NSRPNPILEP GIQSCLTHFN LISHGFGSPA VCAAVTALQN YLTEALKAMD KMYLSNNPNS
HTDNNAKSSD KEEKHRK
