AP2B_MOUSE
ID AP2B_MOUSE Reviewed; 459 AA.
AC Q61313; Q8CEP1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Transcription factor AP-2-beta;
DE Short=AP2-beta;
DE AltName: Full=Activating enhancer-binding protein 2-beta;
GN Name=Tfap2b; Synonyms=Tcfap2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Embryo;
RX PubMed=7555706; DOI=10.1242/dev.121.9.2779;
RA Moser M., Imhof A., Pscherer A., Bauer R., Amselgruber W., Sinowatz F.,
RA Schule R., Buettner R.;
RT "Cloning and characterization of a second AP-2 transcription factor: AP-2
RT beta.";
RL Development 121:2779-2788(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH CITED4.
RX PubMed=12504852; DOI=10.1006/geno.2002.7005;
RA Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T.,
RA Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S.,
RA Shioda T.;
RT "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding
RT transcriptional coactivators: induced expression in mammary epithelial
RT cells.";
RL Genomics 80:601-613(2002).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND SUMOYLATION.
RX PubMed=25187989; DOI=10.1371/journal.pgen.1004499;
RA Williams M.J., Goergen P., Rajendran J., Zheleznyakova G., Haegglund M.G.,
RA Perland E., Bagchi S., Kalogeropoulou A., Khan Z., Fredriksson R.,
RA Schioeth H.B.;
RT "Obesity-linked homologues TfAP-2 and Twz establish meal frequency in
RT Drosophila melanogaster.";
RL PLoS Genet. 10:e1004499-e1004499(2014).
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:0000250|UniProtKB:Q92481}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q92481}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25187989}. 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:0000269|PubMed:25187989}.
CC -!- TISSUE SPECIFICITY: Localizes to neurons in areas of the cerebral
CC cortex, cerebellum and hypothalamus (at protein level).
CC {ECO:0000269|PubMed:25187989}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryo day 9.5 to birth. In day
CC 13.5 embryo, expressed abundantly in cells coating the neural tube.
CC Expression continues posteriorly in the spinal cord, the dorsal root
CC ganglia, in the prevertebal sympathic ganglia and the ganglion nodosum.
CC High expression found in the dorsal and anteriolateral primordium of
CC the midbrain. Expression also found in skin, kidneys and in many areas
CC of the facial mesenchyme. In adults, expressed in the eye, skin,
CC kidney, prostate, thymus, skeletal muscle and, very weakly in the
CC brain. Highest levels found in kidney.
CC -!- INDUCTION: During retinoic acid-mediated differentiation. Up-regulated
CC by starvation and a high fat diet (PubMed:25187989).
CC {ECO:0000269|PubMed:25187989}.
CC -!- PTM: Sumoylated (PubMed:25187989). Sumoylated on Lys-21; which inhibits
CC transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:Q92481, ECO:0000269|PubMed:25187989}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55036.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X78197; CAA55036.1; ALT_INIT; mRNA.
DR EMBL; AK017373; BAB30714.2; -; mRNA.
DR CCDS; CCDS14839.1; -.
DR PIR; S45112; S45112.
DR RefSeq; NP_033360.2; NM_009334.3.
DR AlphaFoldDB; Q61313; -.
DR STRING; 10090.ENSMUSP00000027059; -.
DR iPTMnet; Q61313; -.
DR PhosphoSitePlus; Q61313; -.
DR MaxQB; Q61313; -.
DR PaxDb; Q61313; -.
DR PRIDE; Q61313; -.
DR ProteomicsDB; 281894; -.
DR Antibodypedia; 4175; 382 antibodies from 31 providers.
DR DNASU; 21419; -.
DR Ensembl; ENSMUST00000027059; ENSMUSP00000027059; ENSMUSG00000025927.
DR GeneID; 21419; -.
DR KEGG; mmu:21419; -.
DR UCSC; uc007akr.2; mouse.
DR CTD; 7021; -.
DR MGI; MGI:104672; Tfap2b.
DR VEuPathDB; HostDB:ENSMUSG00000025927; -.
DR eggNOG; KOG3811; Eukaryota.
DR GeneTree; ENSGT00950000182848; -.
DR InParanoid; Q61313; -.
DR OMA; WALLVTY; -.
DR OrthoDB; 641707at2759; -.
DR PhylomeDB; Q61313; -.
DR TreeFam; TF313718; -.
DR Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR BioGRID-ORCS; 21419; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q61313; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61313; protein.
DR Bgee; ENSMUSG00000025927; Expressed in preputial swelling and 191 other tissues.
DR ExpressionAtlas; Q61313; baseline and differential.
DR Genevisible; Q61313; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
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; ISS: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; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0035909; P:aorta morphogenesis; IMP:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0097275; P:cellular ammonium homeostasis; IMP:UniProtKB.
DR GO; GO:0097276; P:cellular creatinine homeostasis; IMP:UniProtKB.
DR GO; GO:0097277; P:cellular urea homeostasis; IMP:UniProtKB.
DR GO; GO:0072044; P:collecting duct development; IMP:UniProtKB.
DR GO; GO:0072017; P:distal tubule development; IMP:UniProtKB.
DR GO; GO:0097070; P:ductus arteriosus closure; IMP:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IEP:UniProtKB.
DR GO; GO:0035136; P:forelimb morphogenesis; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0035137; P:hindlimb morphogenesis; IMP:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0010960; P:magnesium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0072210; P:metanephric nephron development; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0035810; P:positive regulation of urine volume; IMP:UniProtKB.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0003091; P:renal water homeostasis; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0007423; P:sensory organ development; IEP:UniProtKB.
DR GO; GO:0043588; P:skin development; IEP:UniProtKB.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR GO; GO:0055078; P:sodium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0048485; P:sympathetic nervous system development; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
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; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..459
FT /note="Transcription factor AP-2-beta"
FT /id="PRO_0000184802"
FT REGION 30..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..429
FT /note="H-S-H (helix-span-helix), dimerization"
FT REGION 435..459
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:0000250"
SQ SEQUENCE 459 AA; 50373 MW; B1932B329D3D98EE 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 MFLNNTTNRH TSGEGPGSKT GDKEEKHRK
