Q92481 (AP2B_HUMAN) 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	460 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. 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
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 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_component	nucleus Inferred from direct assay PubMed 20607706. Source: UniProtKB
Molecular_function	DNA 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Transcription factor AP-2-beta		PRO_0000184801
Regions
	Compositional bias	41 – 131	91	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) Probable
Natural variations
	Alternative sequence	27	1	E → EMLVHTYSSM in isoform 2.		VSP_006408
	Natural variant	73	1	P → R in CHAR. Ref.12		VAR_016977
	Natural variant	236	1	R → C in CHAR. Ref.12		VAR_016978
	Natural variant	236	1	R → S in CHAR. Ref.12		VAR_016979
	Natural variant	275	1	A → D in CHAR. Ref.11		VAR_011318
	Natural variant	285	1	R → Q in CHAR. Ref.12		VAR_016980
	Natural variant	300	1	R → C in CHAR. Ref.11		VAR_011319
Experimental info
	Sequence conflict	258	1	S → A in CAA71047. Ref.1
	Sequence conflict	362 – 460	99	QLCKE…EKHRK → GNFVKNLRIYWRRTGHR in CAA71047. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: A6420EA0C265DDA2	FASTA	460	50,474
	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
	Isoform 2 [UniParc]. Checksum: C4E0DCC428DBF0F8	FASTA	469	51,524
	10 20 30 40 50 60 MHSPPRDQAA IMLWKLVENV KYEDIYEMLV HTYSSMDRHD GVPSHSSRLS QLGSVSQGPY 70 80 90 100 110 120 SSAPPLSHTP SSDFQPPYFP PPYQPLPYHQ SQDPYSHVND PYSLNPLHQP QQHPWGQRQR 130 140 150 160 170 180 QEVGSEAGSL LPQPRAALPQ LSGLDPRRDY HSVRRPDVLL HSAHHGLDAG MGDSLSLHGL 190 200 210 220 230 240 GHPGMEDVQS VEDANNSGMN LLDQSVIKKV PVPPKSVTSL MMNKDGFLGG MSVNTGEVFC 250 260 270 280 290 300 SVPGRLSLLS STSKYKVTVG EVQRRLSPPE CLNASLLGGV LRRAKSKNGG RSLRERLEKI 310 320 330 340 350 360 GLNLPAGRRK AANVTLLTSL VEGEAVHLAR DFGYICETEF PAKAVSEYLN RQHTDPSDLH 370 380 390 400 410 420 SRKNMLLATK QLCKEFTDLL AQDRTPIGNS RPSPILEPGI QSCLTHFSLI THGFGAPAIC 430 440 450 460 AALTALQNYL TEALKGMDKM FLNNTTTNRH TSGEGPGSKT GDKEEKHRK

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	NP_003212.2. NM_003221.3.
UniGene	Hs.33102.
3D structure databases
ProteinModelPortal	Q92481.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	112879. 11 interactions.
IntAct	Q92481. 4 interactions.
MINT	MINT-1424146.
STRING	9606.ENSP00000377265.
PTM databases
PhosphoSite	Q92481.
Polymorphism databases
DMDM	152031557.
Proteomic databases
PaxDb	Q92481.
PRIDE	Q92481.
Protocols and materials databases
DNASU	7021.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263046; ENSP00000263046; ENSG00000008196. [Q92481-2] ENST00000393655; ENSP00000377265; ENSG00000008196. [Q92481-1]
GeneID	7021.
KEGG	hsa:7021.
UCSC	uc003pag.3. human. [Q92481-1]
Organism-specific databases
CTD	7021.
GeneCards	GC06P050833.
HGNC	HGNC:11743. TFAP2B.
HPA	CAB010426. HPA034683.
MIM	169100. phenotype. 601601. gene.
neXtProt	NX_Q92481.
Orphanet	46627. Char syndrome.
PharmGKB	PA36460.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG300693.
HOVERGEN	HBG002455.
InParanoid	Q92481.
KO	K09176.
OMA	IGHPGME.
OrthoDB	EOG7HHWS1.
PhylomeDB	Q92481.
TreeFam	TF313718.
Gene expression databases
ArrayExpress	Q92481.
Bgee	Q92481.
CleanEx	HS_TFAP2B.
Genevestigator	Q92481.
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
GeneWiki	TFAP2B.
GenomeRNAi	7021.
NextBio	27431.
PRO	Q92481.
SOURCE	Search...

Entry information

Entry name

AP2B_HUMAN

Accession

Primary (citable) accession number: Q92481
Secondary accession number(s): Q5JYX6 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.