AP2E_HUMAN
ID AP2E_HUMAN Reviewed; 442 AA.
AC Q6VUC0; Q8IW12;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Transcription factor AP-2-epsilon;
DE Short=AP2-epsilon;
DE AltName: Full=Activating enhancer-binding protein 2-epsilon;
GN Name=TFAP2E {ECO:0000312|EMBL:CAI23520.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAQ91614.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=14636996; DOI=10.1016/s0378-1119(03)00840-0;
RA Tummala R., Romano R.-A., Fuchs E., Sinha S.;
RT "Molecular cloning and characterization of AP-2 epsilon, a fifth member of
RT the AP-2 family.";
RL Gene 321:93-102(2003).
RN [2] {ECO:0000312|EMBL:CAI23520.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH41175.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus {ECO:0000312|EMBL:AAH41175.1};
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).
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-epsilon
CC may play a role in the development of the CNS and in cartilage
CC differentiation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6VUP9}.
CC -!- TISSUE SPECIFICITY: Expressed in skin, primary keratinocytes,
CC immortalized keratinocytes, and HeLa cell line.
CC {ECO:0000269|PubMed:14636996}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH41175.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAX07409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Activating protein 2 entry;
CC URL="https://en.wikipedia.org/wiki/Activating_protein_2";
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DR EMBL; AY326454; AAQ91614.1; -; mRNA.
DR EMBL; AL157951; CAI23520.1; -; Genomic_DNA.
DR EMBL; AC004865; CAI23520.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX07409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC041175; AAH41175.1; ALT_INIT; mRNA.
DR CCDS; CCDS393.2; -.
DR RefSeq; NP_848643.2; NM_178548.3.
DR AlphaFoldDB; Q6VUC0; -.
DR IntAct; Q6VUC0; 1.
DR STRING; 9606.ENSP00000362332; -.
DR iPTMnet; Q6VUC0; -.
DR PhosphoSitePlus; Q6VUC0; -.
DR BioMuta; TFAP2E; -.
DR DMDM; 74749476; -.
DR EPD; Q6VUC0; -.
DR jPOST; Q6VUC0; -.
DR MassIVE; Q6VUC0; -.
DR MaxQB; Q6VUC0; -.
DR PaxDb; Q6VUC0; -.
DR PeptideAtlas; Q6VUC0; -.
DR PRIDE; Q6VUC0; -.
DR ProteomicsDB; 67731; -.
DR Antibodypedia; 31581; 57 antibodies from 17 providers.
DR DNASU; 339488; -.
DR Ensembl; ENST00000373235.4; ENSP00000362332.3; ENSG00000116819.9.
DR GeneID; 339488; -.
DR KEGG; hsa:339488; -.
DR MANE-Select; ENST00000373235.4; ENSP00000362332.3; NM_178548.4; NP_848643.2.
DR UCSC; uc010ohy.3; human.
DR CTD; 339488; -.
DR DisGeNET; 339488; -.
DR GeneCards; TFAP2E; -.
DR HGNC; HGNC:30774; TFAP2E.
DR HPA; ENSG00000116819; Tissue enhanced (brain).
DR MIM; 614428; gene.
DR neXtProt; NX_Q6VUC0; -.
DR OpenTargets; ENSG00000116819; -.
DR PharmGKB; PA134992283; -.
DR VEuPathDB; HostDB:ENSG00000116819; -.
DR eggNOG; KOG3811; Eukaryota.
DR GeneTree; ENSGT00950000182848; -.
DR HOGENOM; CLU_035175_4_1_1; -.
DR InParanoid; Q6VUC0; -.
DR OMA; QEAGYPH; -.
DR OrthoDB; 641707at2759; -.
DR PhylomeDB; Q6VUC0; -.
DR TreeFam; TF313718; -.
DR PathwayCommons; Q6VUC0; -.
DR Reactome; R-HSA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR BioGRID-ORCS; 339488; 19 hits in 1087 CRISPR screens.
DR GenomeRNAi; 339488; -.
DR Pharos; Q6VUC0; Tbio.
DR PRO; PR:Q6VUC0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6VUC0; protein.
DR Bgee; ENSG00000116819; Expressed in cerebellar hemisphere and 104 other tissues.
DR Genevisible; Q6VUC0; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
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 InterPro; IPR004979; TF_AP2.
DR InterPro; IPR013854; TF_AP2_C.
DR PANTHER; PTHR10812; PTHR10812; 1.
DR Pfam; PF03299; TF_AP-2; 1.
DR PRINTS; PR01748; AP2TNSCPFCT.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..442
FT /note="Transcription factor AP-2-epsilon"
FT /id="PRO_0000309516"
FT REGION 287..417
FT /note="H-S-H (helix-span-helix), dimerization"
FT /evidence="ECO:0000255"
FT MOTIF 54..59
FT /note="PPxY motif"
FT /evidence="ECO:0000255"
FT MOD_RES 246
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P05549"
SQ SEQUENCE 442 AA; 46212 MW; 823209DA7C0EC527 CRC64;
MLVHTYSAME RPDGLGAAAG GARLSSLPQA AYGPAPPLCH TPAATAAAEF QPPYFPPPYP
QPPLPYGQAP DAAAAFPHLA GDPYGGLAPL AQPQPPQAAW AAPRAAARAH EEPPGLLAPP
ARALGLDPRR DYATAVPRLL HGLADGAHGL ADAPLGLPGL AAAPGLEDLQ AMDEPGMSLL
DQSVIKKVPI PSKASSLSAL SLAKDSLVGG ITNPGEVFCS VPGRLSLLSS TSKYKVTVGE
VQRRLSPPEC LNASLLGGVL RRAKSKNGGR CLRERLEKIG LNLPAGRRKA ANVTLLTSLV
EGEAVHLARD FGYVCETEFP AKAAAEYLCR QHADPGELHS RKSMLLAAKQ ICKEFADLMA
QDRSPLGNSR PALILEPGVQ SCLTHFSLIT HGFGGPAICA ALTAFQNYLL ESLKGLDKMF
LSSVGSGHGE TKASEKDAKH RK
