Q61313 (AP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor AP-2-beta
Short name=AP2-beta

Alternative name(s):
Activating enhancer-binding protein 2-beta

Gene names

Name:	Tfap2b
Synonyms:	Tcfap2b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-beta appears to be required for normal face and limb development and for proper terminal differentiation and function of renal tubular epithelia.
Subunit structure	Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity By similarity. Ref.3
Subcellular location	Nucleus Probable.
Developmental stage	Expressed from embryo day 9.5 to birth. In day 13.5 embryo, expressed abundantly in cells coating the neural tube. Expression continues posteriorly in the spinal cord, the dorsal root ganglia, in the prevertebal sympathic ganglia and the ganglion nodosum. High expression found in the dorsal and anteriolateral primordium of the midbrain. Expression also found in skin, kidneys and in many areas of the facial mesenchyme. In adults, expressed in the eye, skin, kidney, prostate, thymus, skeletal muscle and, very weakly in the brain. Highest levels found in kidney.
Induction	During retinoic acid-mediated differentiation.
Post-translational modification	Sumoylated on Lys-21; which inhibits transcriptional activity By similarity.
Sequence similarities	Belongs to the AP-2 family.
Sequence caution	The sequence CAA55036.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aorta morphogenesis Inferred from mutant phenotype PubMed 21829553. Source: UniProtKB calcium ion homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB cellular ammonia homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB cellular creatinine homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB cellular urea homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB collecting duct development Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB distal tubule development Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB ductus arteriosus closure Inferred from mutant phenotype PubMed 21829553. Source: UniProtKB fat cell differentiation Inferred from expression pattern PubMed 15940393. Source: UniProtKB forelimb morphogenesis Inferred from mutant phenotype PubMed 21829553. Source: UniProtKB glucose homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB glucose metabolic process Inferred from sequence or structural similarity. Source: UniProtKB hindlimb morphogenesis Inferred from mutant phenotype PubMed 21829553. Source: UniProtKB magnesium ion homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB metanephric nephron development Inferred from expression pattern Ref.1. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype PubMed 17525748. Source: UniProtKB negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB phosphate ion homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype PubMed 17525748. Source: UniProtKB positive regulation of neuron apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of urine volume Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB potassium ion homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB regulation of BMP signaling pathway Inferred from mutant phenotype PubMed 21829553. Source: UniProtKB regulation of cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of insulin secretion Inferred from sequence or structural similarity. Source: UniProtKB renal water homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB retina layer formation Inferred from electronic annotation. Source: Compara sensory organ development Inferred from expression pattern Ref.1. Source: UniProtKB skin development Inferred from expression pattern Ref.1. Source: UniProtKB sodium ion homeostasis Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB sympathetic nervous system development Inferred from genetic interaction PubMed 21539825. Source: MGI
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay Ref.1. Source: MGI RNA polymerase II core promoter sequence-specific DNA binding Inferred from direct assay PubMed 21829553. Source: UniProtKB RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 21829553. Source: UniProtKB RNA polymerase II transcription coactivator activity Inferred from direct assay PubMed 21829553. Source: UniProtKB RNA polymerase II transcription corepressor activity Inferred from direct assay PubMed 21829553. Source: UniProtKB cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from mutant phenotype PubMed 17525748. Source: UniProtKB enhancer sequence-specific DNA binding Inferred from electronic annotation. Source: Compara protein dimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 459	459	Transcription factor AP-2-beta		PRO_0000184802
Regions
	Region	299 – 429	131	H-S-H (helix-span-helix), dimerization
	Compositional bias	34 – 131	98	Gln/Pro-rich (transactivation domain)
Amino acid modifications
	Modified residue	258	1	Phosphoserine; by PKA By similarity
	Cross-link	21		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q61313 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: B1932B329D3D98EE	FASTA	459	50,373
	10 20 30 40 50 60 MHSPPRDQAA IMLWKLVENV KYEDIYEDRH DGVPSHSSRL SQLGSVSQGP YSSAPPLSHT 70 80 90 100 110 120 PSSDFQPPYF PPPYQPLPYH QSQDPYSHVN DPYSLNPLHQ PQQHPWGQRQ RQEVGSEAGS 130 140 150 160 170 180 LLPQPRAALP QLSGLDPRRD YHSVRRPDVL LHSAHHGLDA GMGDSLSLHG LGHPGMEDVQ 190 200 210 220 230 240 SVEDANNSGM NLLDQSVIKK VPVPPKSVTS LMMNKDGFLG GMSVNTGEVF CSVPGRLSLL 250 260 270 280 290 300 SSTSKYKVTV GEVQRRLSPP ECLNASLLGG VLRRAKSKNG GRSLRERLEK IGLNLPAGRR 310 320 330 340 350 360 KAANVTLLTS LVEGEAVHLA RDFGYICETE FPAKAVSEYL NRQHTDPSDL HSRKNMLLAT 370 380 390 400 410 420 KQLCKEFTDL LAQDRTPIGN SRPSPILEPG IQSCLTHFSL ITHGFGAPAI CAALTALQNY 430 440 450 LTEALKGMDK MFLNNTTNRH TSGEGPGSKT GDKEEKHRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a second AP-2 transcription factor: AP-2 beta." Moser M., Imhof A., Pscherer A., Bauer R., Amselgruber W., Sinowatz F., Schule R., Buettner R. Development 121:2779-2788(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Embryo.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head.
[3]	"Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding transcriptional coactivators: induced expression in mammary epithelial cells." Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T., Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S., Shioda T. Genomics 80:601-613(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CITED4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X78197 mRNA. Translation: CAA55036.1. Different initiation. AK017373 mRNA. Translation: BAB30714.2.
IPI	IPI00119910.
PIR	S45112.
RefSeq	NP_001020476.1. NM_001025305.1. NP_033360.2. NM_009334.2.
UniGene	Mm.137021.
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q61313.
Proteomic databases
PRIDE	Q61313.
Protocols and materials databases
DNASU	21419.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027059; ENSMUSP00000027059; ENSMUSG00000025927.
GeneID	21419.
KEGG	mmu:21419.
UCSC	uc007akr.1. mouse.
Organism-specific databases
CTD	7021.
MGI	MGI:104672. Tfap2b.
Phylogenomic databases
eggNOG	NOG300693.
GeneTree	ENSGT00550000074577.
HOGENOM	HOG000231737.
HOVERGEN	HBG002455.
InParanoid	Q61313.
KO	K09176.
OMA	IGHPGME.
OrthoDB	EOG4Z0B5M.
Gene expression databases
ArrayExpress	Q61313.
Bgee	Q61313.
CleanEx	MM_TCFAP2B.
Genevestigator	Q61313.
GermOnline	ENSMUSG00000025927. Mus musculus.
Family and domain databases
InterPro	IPR004979. TF_AP2. IPR008122. TF_AP2_beta. IPR013854. TF_AP2_C. [Graphical view]
PANTHER	PTHR10812. PTHR10812. 1 hit.
Pfam	PF03299. TF_AP-2. 1 hit. [Graphical view]
PRINTS	PR01750. AP2BTNSCPFCT. PR01748. AP2TNSCPFCT.
ProtoNet	Search...
Other
NextBio	300728.
SOURCE	Search...

Entry information

Entry name

AP2B_MOUSE

Accession

Primary (citable) accession number: Q61313
Secondary accession number(s): Q8CEP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	July 10, 2007
Last modified:	April 3, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program