Reviewed, UniProtKB/Swiss-Prot Q61313 (AP2B_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	kidney development Inferred from mutant phenotype. Source: MGI positive regulation of transcription from RNA polymerase II promoter, global Inferred from sequence or structural similarity. Source: HGNC transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein dimerization activity Inferred from sequence or structural similarity. Source: HGNC sequence-specific DNA binding Inferred from sequence or structural similarity. Source: HGNC transcription factor activity Inferred from sequence or structural similarity. Source: HGNC
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)
	Q61313-1 [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: 7555706] [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: 16141072] [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: 12504852] [Abstract] Cited for: INTERACTION WITH CITED4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X78197 mRNA. Translation: CAA55036.1. Different initiation. AK017373 mRNA. Translation: BAB30714.2.
IPI	IPI00119910.
PIR	S45112.
RefSeq	NP_033360.2.
UniGene	Mm.137021
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q61313.
Genome annotation databases
Ensembl	ENSMUSG00000025927. Mus musculus. [Contig view]
GeneID	21419.
Organism-specific databases
MGI	MGI:104672. Tcfap2b.
Phylogenomic databases
HOVERGEN	Q61313.
OMA	Q61313. FRAKSKN.
Gene expression databases
ArrayExpress	Q61313.
Bgee	Q61313.
CleanEx	MM_TCFAP2B.
GermOnline	ENSMUSG00000025927. Mus musculus.
Family and domain databases
InterPro	IPR004979. TF_AP2. IPR008122. TF_AP2_beta_N. IPR013854. TF_AP2_C. [Graphical view]
PANTHER	PTHR10812. TF_AP2. 1 hit.
Pfam	PF03299. TF_AP-2. 1 hit. [Graphical view]
PRINTS	PR01750. AP2BTNSCPFCT. PR01748. AP2TNSCPFCT.
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)