AP2B_HUMAN
ID AP2B_HUMAN Reviewed; 460 AA.
AC Q92481; Q5JYX6; Q9NQ63; Q9NU99; Q9UJI7; Q9Y214; Q9Y3K3;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Transcription factor AP-2-beta;
DE Short=AP2-beta;
DE AltName: Full=Activating enhancer-binding protein 2-beta;
GN Name=TFAP2B;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9271117; DOI=10.1101/gad.11.15.1938;
RA Moser M., Buettner R.;
RT "Enhanced apoptotic cell death of renal epithelial cells in mice lacking
RT transcription factor AP-2beta.";
RL Genes Dev. 11:1938-1948(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RA Hasleton M.D., Skinner A., Hurst H.C.;
RT "Characterisation of the human AP-2beta and AP-2gamma genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-460 (ISOFORM 1).
RC TISSUE=Mammary tumor;
RX PubMed=8661133; DOI=10.1006/geno.1996.0351;
RA Williamson J.A., Bosher J.M., Skinner A., Sheer D., Williams T.,
RA Hurst H.C.;
RT "Chromosomal mapping of the human and mouse homologues of two new members
RT of the AP-2 family of transcription factors.";
RL Genomics 35:262-264(1996).
RN [6]
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 [7]
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 [8]
RP INTERACTION WITH UBE2I, AND SUMOYLATION AT LYS-21.
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 [9]
RP INTERACTION WITH CITED2.
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 [10]
RP INVOLVEMENT IN CHAR.
RX PubMed=15684060; DOI=10.1073/pnas.0409852102;
RA Mani A., Radhakrishnan J., Farhi A., Carew K.S., Warnes C.A.,
RA Nelson-Williams C., Day R.W., Pober B., State M.W., Lifton R.P.;
RT "Syndromic patent ductus arteriosus: evidence for haploinsufficient TFAP2B
RT mutations and identification of a linked sleep disorder.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2975-2979(2005).
RN [11]
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 [12]
RP INVOLVEMENT IN PDA2.
RX PubMed=18752453; DOI=10.1089/gte.2008.0015;
RA Khetyar M., Syrris P., Tinworth L., Abushaban L., Carter N.;
RT "Novel TFAP2B mutation in nonsyndromic patent ductus arteriosus.";
RL Genet. Test. 12:457-459(2008).
RN [13]
RP INVOLVEMENT IN PDA2.
RX PubMed=21643846; DOI=10.1007/s00246-011-0024-7;
RA Chen Y.W., Zhao W., Zhang Z.F., Fu Q., Shen J., Zhang Z., Ji W., Wang J.,
RA Li F.;
RT "Familial nonsyndromic patent ductus arteriosus caused by mutations in
RT TFAP2B.";
RL Pediatr. Cardiol. 32:958-965(2011).
RN [14]
RP VARIANTS CHAR ASP-275 AND CYS-300.
RX PubMed=10802654; DOI=10.1038/75578;
RA Satoda M., Zhao F., Diaz G.A., Burn J., Goodship J., Davidson H.R.,
RA Pierpont M.E.M., Gelb B.D.;
RT "Mutations in TFAP2B cause Char syndrome, a familial form of patent ductus
RT arteriosus.";
RL Nat. Genet. 25:42-46(2000).
RN [15]
RP VARIANTS CHAR ARG-73; CYS-236; SER-236 AND GLN-285.
RX PubMed=11505339; DOI=10.1086/323410;
RA Zhao F., Weismann C.G., Satoda M., Pierpont M.E.M., Sweeney E.,
RA Thompson E.M., Gelb B.D.;
RT "Novel TFAP2B mutations that cause Char syndrome provide a genotype-
RT phenotype correlation.";
RL Am. J. Hum. Genet. 69:695-703(2001).
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-beta
CC appears to be required for normal face and limb development and for
CC proper terminal differentiation and function of renal tubular
CC epithelia. {ECO:0000269|PubMed:11694877}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members. Interacts with CITED4. Interacts with UBE2I.
CC Interacts with KCTD1; this interaction represses transcription
CC activation. Interacts with CITED2 (via C-terminus); the interaction
CC stimulates TFAP2B-transcriptional activity.
CC {ECO:0000269|PubMed:11694877, ECO:0000269|PubMed:11744733,
CC ECO:0000269|PubMed:12072434, ECO:0000269|PubMed:12586840,
CC ECO:0000269|PubMed:19115315}.
CC -!- INTERACTION:
CC Q92481; Q92993: KAT5; NbExp=3; IntAct=EBI-725275, EBI-399080;
CC Q92481; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-725275, EBI-11742507;
CC Q92481; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-725275, EBI-9090795;
CC Q92481; P61981: YWHAG; NbExp=3; IntAct=EBI-725275, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61313}. Note=In
CC the brain, localizes to the arcuate hypothalamic nucleus, the
CC ventromedial hypothalamic nucleus and the accumbens nucleus of the
CC ventral striatum. {ECO:0000250|UniProtKB:Q61313}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92481-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92481-2; Sequence=VSP_006408;
CC -!- PTM: Sumoylated on Lys-21; which inhibits transcriptional activity.
CC {ECO:0000305|PubMed:12072434}.
CC -!- DISEASE: Char syndrome (CHAR) [MIM:169100]: An autosomal dominant
CC disorder characterized by patent ductus arteriosus (PDA), facial
CC dysmorphism and hand anomalies. {ECO:0000269|PubMed:10802654,
CC ECO:0000269|PubMed:11505339, ECO:0000269|PubMed:15684060}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Patent ductus arteriosus 2 (PDA2) [MIM:617035]: A congenital
CC heart defect characterized by the persistent opening of fetal ductus
CC arteriosus that fails to close after birth. Fetal ductus arteriosus
CC connects the pulmonary artery to the descending aorta, allowing
CC unoxygenated blood to bypass the lung and flow to the placenta.
CC Normally, the ductus occludes shortly after birth.
CC {ECO:0000269|PubMed:18752453, ECO:0000269|PubMed:21643846}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64990.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA71047.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC01130.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; Y09912; CAA71047.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL031224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037225; AAH37225.2; -; mRNA.
DR EMBL; AJ278356; CAC01130.1; ALT_INIT; Genomic_DNA.
DR EMBL; X95694; CAA64990.1; ALT_INIT; mRNA.
DR CCDS; CCDS4934.2; -. [Q92481-1]
DR RefSeq; NP_003212.2; NM_003221.3. [Q92481-1]
DR RefSeq; XP_011513139.1; XM_011514837.2. [Q92481-2]
DR AlphaFoldDB; Q92481; -.
DR BioGRID; 112879; 19.
DR IntAct; Q92481; 10.
DR STRING; 9606.ENSP00000377265; -.
DR GlyGen; Q92481; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92481; -.
DR PhosphoSitePlus; Q92481; -.
DR BioMuta; TFAP2B; -.
DR DMDM; 152031557; -.
DR EPD; Q92481; -.
DR jPOST; Q92481; -.
DR MassIVE; Q92481; -.
DR MaxQB; Q92481; -.
DR PaxDb; Q92481; -.
DR PeptideAtlas; Q92481; -.
DR PRIDE; Q92481; -.
DR ProteomicsDB; 75261; -. [Q92481-1]
DR ProteomicsDB; 75262; -. [Q92481-2]
DR Antibodypedia; 4175; 382 antibodies from 31 providers.
DR DNASU; 7021; -.
DR Ensembl; ENST00000393655.4; ENSP00000377265.2; ENSG00000008196.13. [Q92481-1]
DR GeneID; 7021; -.
DR KEGG; hsa:7021; -.
DR MANE-Select; ENST00000393655.4; ENSP00000377265.2; NM_003221.4; NP_003212.2.
DR UCSC; uc003pag.4; human. [Q92481-1]
DR CTD; 7021; -.
DR DisGeNET; 7021; -.
DR GeneCards; TFAP2B; -.
DR GeneReviews; TFAP2B; -.
DR HGNC; HGNC:11743; TFAP2B.
DR HPA; ENSG00000008196; Tissue enhanced (epididymis, retina).
DR MalaCards; TFAP2B; -.
DR MIM; 169100; phenotype.
DR MIM; 601601; gene.
DR MIM; 617035; phenotype.
DR neXtProt; NX_Q92481; -.
DR OpenTargets; ENSG00000008196; -.
DR Orphanet; 46627; Char syndrome.
DR Orphanet; 466729; Familial patent arterial duct.
DR PharmGKB; PA36460; -.
DR VEuPathDB; HostDB:ENSG00000008196; -.
DR eggNOG; KOG3811; Eukaryota.
DR GeneTree; ENSGT00950000182848; -.
DR HOGENOM; CLU_035175_4_1_1; -.
DR InParanoid; Q92481; -.
DR OMA; WALLVTY; -.
DR OrthoDB; 641707at2759; -.
DR PhylomeDB; Q92481; -.
DR TreeFam; TF313718; -.
DR PathwayCommons; Q92481; -.
DR Reactome; R-HSA-3232118; SUMOylation of transcription factors.
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 Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR SignaLink; Q92481; -.
DR SIGNOR; Q92481; -.
DR BioGRID-ORCS; 7021; 20 hits in 1097 CRISPR screens.
DR ChiTaRS; TFAP2B; human.
DR GeneWiki; TFAP2B; -.
DR GenomeRNAi; 7021; -.
DR Pharos; Q92481; Tbio.
DR PRO; PR:Q92481; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q92481; protein.
DR Bgee; ENSG00000008196; Expressed in corpus epididymis and 88 other tissues.
DR ExpressionAtlas; Q92481; baseline and differential.
DR Genevisible; Q92481; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
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:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0035909; P:aorta morphogenesis; ISS:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0097275; P:cellular ammonium homeostasis; ISS:UniProtKB.
DR GO; GO:0097276; P:cellular creatinine homeostasis; ISS:UniProtKB.
DR GO; GO:0097277; P:cellular urea homeostasis; ISS:UniProtKB.
DR GO; GO:0072044; P:collecting duct development; ISS:UniProtKB.
DR GO; GO:0072017; P:distal tubule development; ISS:UniProtKB.
DR GO; GO:0097070; P:ductus arteriosus closure; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IEP:UniProtKB.
DR GO; GO:0035136; P:forelimb morphogenesis; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IMP:UniProtKB.
DR GO; GO:0035137; P:hindlimb morphogenesis; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0072210; P:metanephric nephron development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
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:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0055062; P:phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:HGNC-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:GO_Central.
DR GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR GO; GO:0055075; P:potassium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; ISS: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:0050796; P:regulation of insulin secretion; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0003091; P:renal water homeostasis; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEP:UniProtKB.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0055078; P:sodium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0048485; P:sympathetic nervous system development; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR InterPro; IPR004979; TF_AP2.
DR InterPro; IPR008122; TF_AP2_beta.
DR InterPro; IPR013854; TF_AP2_C.
DR PANTHER; PTHR10812; PTHR10812; 1.
DR PANTHER; PTHR10812:SF14; PTHR10812:SF14; 1.
DR Pfam; PF03299; TF_AP-2; 1.
DR PRINTS; PR01750; AP2BTNSCPFCT.
DR PRINTS; PR01748; AP2TNSCPFCT.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Disease variant; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..460
FT /note="Transcription factor AP-2-beta"
FT /id="PRO_0000184801"
FT REGION 30..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
FT VAR_SEQ 27
FT /note="E -> EMLVHTYSSM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006408"
FT VARIANT 73
FT /note="P -> R (in CHAR; dbSNP:rs80338910)"
FT /evidence="ECO:0000269|PubMed:11505339"
FT /id="VAR_016977"
FT VARIANT 236
FT /note="R -> C (in CHAR; dbSNP:rs80338912)"
FT /evidence="ECO:0000269|PubMed:11505339"
FT /id="VAR_016978"
FT VARIANT 236
FT /note="R -> S (in CHAR; dbSNP:rs80338912)"
FT /evidence="ECO:0000269|PubMed:11505339"
FT /id="VAR_016979"
FT VARIANT 275
FT /note="A -> D (in CHAR; dbSNP:rs80338914)"
FT /evidence="ECO:0000269|PubMed:10802654"
FT /id="VAR_011318"
FT VARIANT 285
FT /note="R -> Q (in CHAR; dbSNP:rs80338915)"
FT /evidence="ECO:0000269|PubMed:11505339"
FT /id="VAR_016980"
FT VARIANT 300
FT /note="R -> C (in CHAR; dbSNP:rs80338917)"
FT /evidence="ECO:0000269|PubMed:10802654"
FT /id="VAR_011319"
FT CONFLICT 258
FT /note="S -> A (in Ref. 1; CAA71047)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..460
FT /note="QLCKEFTDLLAQDRTPIGNSRPSPILEPGIQSCLTHFSLITHGFGAPAICAA
FT LTALQNYLTEALKGMDKMFLNNTTTNRHTSGEGPGSKTGDKEEKHRK -> GNFVKNLR
FT IYWRRTGHR (in Ref. 1; CAA71047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50474 MW; A6420EA0C265DDA2 CRC64;
MHSPPRDQAA IMLWKLVENV KYEDIYEDRH DGVPSHSSRL SQLGSVSQGP YSSAPPLSHT
PSSDFQPPYF PPPYQPLPYH QSQDPYSHVN DPYSLNPLHQ PQQHPWGQRQ RQEVGSEAGS
LLPQPRAALP QLSGLDPRRD YHSVRRPDVL LHSAHHGLDA GMGDSLSLHG LGHPGMEDVQ
SVEDANNSGM NLLDQSVIKK VPVPPKSVTS LMMNKDGFLG GMSVNTGEVF CSVPGRLSLL
SSTSKYKVTV GEVQRRLSPP ECLNASLLGG VLRRAKSKNG GRSLRERLEK IGLNLPAGRR
KAANVTLLTS LVEGEAVHLA RDFGYICETE FPAKAVSEYL NRQHTDPSDL HSRKNMLLAT
KQLCKEFTDL LAQDRTPIGN SRPSPILEPG IQSCLTHFSL ITHGFGAPAI CAALTALQNY
LTEALKGMDK MFLNNTTTNR HTSGEGPGSK TGDKEEKHRK
