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Q92481 (AP2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length460 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. Ref.6

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus Probable.

Post-translational modification

Sumoylated on Lys-21; which inhibits transcriptional activity Probable. Ref.8

Involvement in disease

Char syndrome (CHAR) [MIM:169100]: An autosomal dominant disorder characterized by patent ductus arteriosus (PDA), facial dysmorphism and hand anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12

Sequence similarities

Belongs to the AP-2 family.

Sequence caution

The sequence CAA64990.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA71047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB41305.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAC01130.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaorta morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular ammonia homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular creatinine homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular urea homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

collecting duct development

Inferred from sequence or structural similarity. Source: UniProtKB

distal tubule development

Inferred from sequence or structural similarity. Source: UniProtKB

ductus arteriosus closure

Inferred from sequence or structural similarity. Source: UniProtKB

fat cell differentiation

Inferred from expression pattern PubMed 16373396. Source: UniProtKB

forelimb morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

glucose homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

glucose metabolic process

Inferred from mutant phenotype PubMed 15940393PubMed 16373396PubMed 19325541. Source: UniProtKB

hindlimb morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

kidney development

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric nephron development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 17525748. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 20607706. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7559606. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 20607706. Source: UniProtKB

phosphate ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 17525748. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from direct assay PubMed 20607706. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7555706. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of urine volume

Inferred from sequence or structural similarity. Source: UniProtKB

potassium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of BMP signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell differentiation

Inferred from direct assay PubMed 20607706. Source: UniProtKB

regulation of insulin secretion

Inferred from mutant phenotype PubMed 15940393PubMed 19325541. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12169688. Source: HGNC

renal water homeostasis

Inferred from sequence or structural similarity. 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 expression pattern PubMed 20607706. Source: UniProtKB

skin development

Inferred from electronic annotation. Source: Ensembl

sodium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

sympathetic nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleus

Inferred from direct assay PubMed 20607706. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.8. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 7555706. Source: UniProtKB

RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 16373396. Source: UniProtKB

protein dimerization activity

Inferred from direct assay Ref.8. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.12. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.12. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 7555706. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.12PubMed 16373396. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 7555706. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay PubMed 7559606. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92481-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q92481-2)

The sequence of this isoform differs from the canonical sequence as follows:
     27-27: E → EMLVHTYSSM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Transcription factor AP-2-beta
PRO_0000184801

Regions

Compositional bias41 – 13191Gln/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) Probable

Natural variations

Alternative sequence271E → EMLVHTYSSM in isoform 2.
VSP_006408
Natural variant731P → R in CHAR. Ref.12
VAR_016977
Natural variant2361R → C in CHAR. Ref.12
VAR_016978
Natural variant2361R → S in CHAR. Ref.12
VAR_016979
Natural variant2751A → D in CHAR. Ref.11
VAR_011318
Natural variant2851R → Q in CHAR. Ref.12
VAR_016980
Natural variant3001R → C in CHAR. Ref.11
VAR_011319

Experimental info

Sequence conflict2581S → A in CAA71047. Ref.1
Sequence conflict362 – 46099QLCKE…EKHRK → GNFVKNLRIYWRRTGHR in CAA71047. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: A6420EA0C265DDA2

FASTA46050,474
        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        460 
LTEALKGMDK MFLNNTTTNR HTSGEGPGSK TGDKEEKHRK 

« Hide

Isoform 2 [UniParc].

Checksum: C4E0DCC428DBF0F8
Show »

FASTA46951,524

References

« Hide 'large scale' references
[1]"Enhanced apoptotic cell death of renal epithelial cells in mice lacking transcription factor AP-2beta."
Moser M., Buettner R.
Genes Dev. 11:1938-1948(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[4]"Characterisation of the human AP-2beta and AP-2gamma genes."
Hasleton M.D., Skinner A., Hurst H.C.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
[5]"Chromosomal mapping of the human and mouse homologues of two new members of the AP-2 family of transcription factors."
Williamson J.A., Bosher J.M., Skinner A., Sheer D., Williams T., Hurst H.C.
Genomics 35:262-264(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-460 (ISOFORM 1).
Tissue: Mammary tumor.
[6]"Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator."
Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I., Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.
Nat. Genet. 29:469-474(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CITED2.
[7]"Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2."
Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S.
J. Biol. Chem. 277:8559-8565(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CITED4.
[8]"Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo."
Eloranta J.J., Hurst H.C.
J. Biol. Chem. 277:30798-30804(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE2I, SUMOYLATION AT LYS-21.
[9]"Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2."
Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C., Bhattacharya S.
J. Biol. Chem. 278:16021-16029(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CITED2.
[10]"The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivation."
Ding X., Luo C., Zhou J., Zhong Y., Hu X., Zhou F., Ren K., Gan L., He A., Zhu J., Gao X., Zhang J.
J. Cell. Biochem. 106:285-295(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCTD1.
[11]"Mutations in TFAP2B cause Char syndrome, a familial form of patent ductus arteriosus."
Satoda M., Zhao F., Diaz G.A., Burn J., Goodship J., Davidson H.R., Pierpont M.E.M., Gelb B.D.
Nat. Genet. 25:42-46(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHAR ASP-275 AND CYS-300.
[12]"Novel TFAP2B mutations that cause Char syndrome provide a genotype-phenotype correlation."
Zhao F., Weismann C.G., Satoda M., Pierpont M.E.M., Sweeney E., Thompson E.M., Gelb B.D.
Am. J. Hum. Genet. 69:695-703(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHAR ARG-73; CYS-236; SER-236 AND GLN-285.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Activatin protein 2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09912 Genomic DNA. Translation: CAA71047.1. Different initiation.
AL031224 Genomic DNA. Translation: CAB41305.1. Different initiation.
AL031224, AL049693 Genomic DNA. Translation: CAI20235.2.
AL049693 Genomic DNA. Translation: CAB89563.3.
BC037225 mRNA. Translation: AAH37225.2.
AJ278356 Genomic DNA. Translation: CAC01130.1. Different initiation.
X95694 mRNA. Translation: CAA64990.1. Different initiation.
RefSeqNP_003212.2. NM_003221.3.
UniGeneHs.33102.

3D structure databases

ProteinModelPortalQ92481.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112879. 11 interactions.
IntActQ92481. 4 interactions.
MINTMINT-1424146.
STRING9606.ENSP00000377265.

PTM databases

PhosphoSiteQ92481.

Polymorphism databases

DMDM152031557.

Proteomic databases

PaxDbQ92481.
PRIDEQ92481.

Protocols and materials databases

DNASU7021.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263046; ENSP00000263046; ENSG00000008196. [Q92481-2]
ENST00000393655; ENSP00000377265; ENSG00000008196. [Q92481-1]
GeneID7021.
KEGGhsa:7021.
UCSCuc003pag.3. human. [Q92481-1]

Organism-specific databases

CTD7021.
GeneCardsGC06P050833.
HGNCHGNC:11743. TFAP2B.
HPACAB010426.
HPA034683.
MIM169100. phenotype.
601601. gene.
neXtProtNX_Q92481.
Orphanet46627. Char syndrome.
PharmGKBPA36460.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300693.
HOVERGENHBG002455.
InParanoidQ92481.
KOK09176.
OMAIGHPGME.
OrthoDBEOG7HHWS1.
PhylomeDBQ92481.
TreeFamTF313718.

Gene expression databases

ArrayExpressQ92481.
BgeeQ92481.
CleanExHS_TFAP2B.
GenevestigatorQ92481.

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

GeneWikiTFAP2B.
GenomeRNAi7021.
NextBio27431.
PROQ92481.
SOURCESearch...

Entry information

Entry nameAP2B_HUMAN
AccessionPrimary (citable) accession number: Q92481
Secondary accession number(s): Q5JYX6 expand/collapse secondary AC list , Q9NQ63, Q9NU99, Q9UJI7, Q9Y214, Q9Y3K3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM