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Q61313 (AP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaorta 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

kidney development

Inferred from mutant phenotype PubMed 9271117. Source: MGI

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

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 17525748. Source: GOC

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 21539825. Source: MGI

negative regulation of transcription, DNA-templated

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 transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21829553. 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

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

renal water homeostasis

Inferred from mutant phenotype PubMed 12695560. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to lithium ion

Inferred from electronic annotation. Source: Ensembl

retina layer formation

Inferred from electronic annotation. Source: Ensembl

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

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21829553. Source: UniProtKB

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionRNA 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

chromatin binding

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

protein dimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Transcription factor AP-2-beta
PRO_0000184802

Regions

Region299 – 429131H-S-H (helix-span-helix), dimerization
Compositional bias34 – 13198Gln/Pro-rich (transactivation domain)

Amino acid modifications

Modified residue2581Phosphoserine; by PKA By similarity
Cross-link21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q61313 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: B1932B329D3D98EE

FASTA45950,373
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRS45112.
RefSeqNP_033360.2. NM_009334.3.
UniGeneMm.137021.

3D structure databases

ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ61313.

Proteomic databases

PRIDEQ61313.

Protocols and materials databases

DNASU21419.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027059; ENSMUSP00000027059; ENSMUSG00000025927.
GeneID21419.
KEGGmmu:21419.
UCSCuc007akr.1. mouse.

Organism-specific databases

CTD7021.
MGIMGI:104672. Tfap2b.

Phylogenomic databases

eggNOGNOG300693.
GeneTreeENSGT00550000074577.
HOGENOMHOG000231737.
HOVERGENHBG002455.
InParanoidQ61313.
KOK09176.
OMAIGHPGME.
OrthoDBEOG7HHWS1.
PhylomeDBQ61313.
TreeFamTF313718.

Gene expression databases

BgeeQ61313.
CleanExMM_TCFAP2B.
GenevestigatorQ61313.

Family and domain databases

InterProIPR004979. TF_AP2.
IPR008122. TF_AP2_beta.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERPTHR10812. PTHR10812. 1 hit.
PfamPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSPR01750. AP2BTNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNetSearch...

Other

NextBio300728.
PROQ61313.
SOURCESearch...

Entry information

Entry nameAP2B_MOUSE
AccessionPrimary (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 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot