P05549 (AP2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
AP-2 transcription factor
Activating enhancer-binding protein 2-alpha
Activator protein 2
Short name=AP-2

Gene names

Name:	TFAP2A
Synonyms:	AP2TF, TFAP2

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	437 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-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region. Ref.9 Ref.12
Subunit structure	Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with WWOX. Interacts with CITED4. Interacts with UBE2I. Interacts with RALBP1 in a complex also containing EPN1 and NUMB during interphase and mitosis. Interacts with KCTD1; this interaction represses transcription activation. Interacts (via C-terminus) with CITED2 (via C-terminus); the interaction stimulates TFAP2A-transcriptional activation. Interacts (via N-terminus) with EP300 (via N-terminus); the interaction requires CITED2. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16
Subcellular location	Nucleus Ref.12.
Domain	The WW-binding motif mediates interaction with WWOX By similarity. Ref.14
Post-translational modification	Sumoylated on Lys-10; which inhibits transcriptional activity Probable. Ref.11
Involvement in disease	Branchiooculofacial syndrome (BOFS) [MIM:113620]: A syndrome characterized by growth retardation, bilateral branchial sinus defects with hemangiomatous, scarred skin, cleft lip with or without cleft palate, pseudocleft of the upper lip, nasolacrimal duct obstruction, low set ears with posterior rotation, a malformed, asymmetrical nose with a broad bridge and flattened tip, conductive or sensorineural deafness, ocular and renal anomalies. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17
Sequence similarities	Belongs to the AP-2 family.

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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anterior neuropore closure Inferred from electronic annotation. Source: Compara basement membrane organization Inferred from electronic annotation. Source: Compara bone morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB cellular response to iron ion Inferred from direct assay PubMed 20808827. Source: UniProtKB cornea development in camera-type eye Inferred from electronic annotation. Source: Compara embryonic body morphogenesis Inferred from electronic annotation. Source: Compara embryonic cranial skeleton morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB embryonic forelimb morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB embryonic pattern specification Inferred from electronic annotation. Source: Compara epidermis morphogenesis Inferred from electronic annotation. Source: Compara eyelid development in camera-type eye Inferred from sequence or structural similarity. Source: UniProtKB face morphogenesis Inferred from electronic annotation. Source: Compara forebrain neuron development Inferred from electronic annotation. Source: Compara inner ear morphogenesis Inferred from mutant phenotype PubMed 21204207. Source: UniProtKB keratinocyte development Inferred from electronic annotation. Source: Compara kidney development Inferred from mutant phenotype PubMed 21204207. Source: UniProtKB lens induction in camera-type eye Inferred from electronic annotation. Source: Compara metanephric nephron development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay PubMed 20066163. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay PubMed 20607706. Source: UniProtKB negative regulation of epidermal growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of reactive oxygen species metabolic process Inferred from direct assay PubMed 20066163. Source: UniProtKB negative regulation of transcription by competitive promoter binding Inferred from direct assay Ref.2. Source: UniProtKB neural crest cell development Inferred from electronic annotation. Source: Compara oculomotor nerve formation Inferred from sequence or structural similarity. Source: UniProtKB optic cup structural organization Inferred from sequence or structural similarity. Source: UniProtKB optic vesicle morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB outflow tract morphogenesis Inferred from electronic annotation. Source: Compara palate development Inferred from mutant phenotype PubMed 21204207. Source: UniProtKB positive regulation of bone mineralization Inferred from direct assay PubMed 19578371. Source: UniProtKB positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of neuron apoptotic process Inferred from direct assay PubMed 20607706. Source: UniProtKB positive regulation of tooth mineralization Inferred from direct assay PubMed 19578371. Source: UniProtKB regulation of cell differentiation Inferred from direct assay PubMed 20607706. Source: UniProtKB regulation of neuron differentiation Inferred from electronic annotation. Source: Compara retina layer formation Inferred from expression pattern PubMed 20607706. Source: UniProtKB sensory perception of sound Inferred from mutant phenotype PubMed 21204207. Source: UniProtKB skin development Inferred from electronic annotation. Source: Compara sympathetic nervous system development Inferred from electronic annotation. Source: Compara trigeminal nerve development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA centrosome Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.16PubMed 20607706. Source: UniProtKB
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 21084835PubMed 9520389. Source: UniProtKB RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from direct assay PubMed 11278550PubMed 20066163PubMed 9520389. Source: UniProtKB RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 11278550PubMed 20808827. Source: UniProtKB RNA polymerase II core promoter sequence-specific DNA binding Inferred from direct assay PubMed 7555706. Source: UniProtKB RNA polymerase II distal enhancer sequence-specific DNA binding Inferred from electronic annotation. Source: Compara RNA polymerase II transcription coactivator activity Inferred from electronic annotation. Source: Compara RNA polymerase II transcription corepressor activity Inferred from electronic annotation. Source: Compara chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Traceable author statement PubMed 7559606. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay Ref.2. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.12PubMed 7555706Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EP300	Q09472	7	EBI-347351,EBI-447295

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: P05549-1)

Also known as: AP-2A;

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: P05549-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MLWKLTDNIKYEDCE → MLVHSFSAM

Note: No experimental confirmation available.

Isoform 4 (identifier: P05549-2)

Also known as: AP-2B;

The sequence of this isoform differs from the canonical sequence as follows:
     296-437: EAVHLARDFG...SSDKEEKHRK → KRIHLLTRRN...SILLPSFPLP

Note: May be an aberrantly processed form with no significant distribution in vivo.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 437	437	Transcription factor AP-2-alpha		PRO_0000184796
Regions
	Region	280 – 410	131	H-S-H (helix-span-helix), dimerization
	Motif	57 – 62	6	WW-binding
	Compositional bias	29 – 117	89	Gln/Pro-rich (transactivation domain)
Amino acid modifications
	Modified residue	239	1	Phosphoserine; by PKA
	Cross-link	10		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Natural variations
	Alternative sequence	1 – 15	15	MLWKL…YEDCE → MLVHSFSAM in isoform 2.		VSP_043268
	Alternative sequence	296 – 437	142	EAVHL…EKHRK → KRIHLLTRRNFLLGKWIIFS GQMFGRILCQLGSFIFAENI ARCEWNYFMAKRNICMYSYT SILLPSFPLP in isoform 4.		VSP_006401
	Natural variant	249	1	L → P in BOFS. Ref.17		VAR_045838
	Natural variant	254	1	R → G in BOFS. Ref.17		VAR_045839
	Natural variant	255	1	R → G in BOFS. Ref.17		VAR_045840
	Natural variant	262	1	G → E in BOFS. Ref.17		VAR_045841
Experimental info
	Mutagenesis	239	1	S → A: No phosphorylation. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (AP-2A) [UniParc]. Last modified July 1, 1989. Version 1. Checksum: FB8FA33C3AEED71F	FASTA	437	48,062
	10 20 30 40 50 60 MLWKLTDNIK YEDCEDRHDG TSNGTARLPQ LGTVGQSPYT SAPPLSHTPN ADFQPPYFPP 70 80 90 100 110 120 PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR QSQESGLLHT HRGLPHQLSG 130 140 150 160 170 180 LDPRRDYRRH EDLLHGPHAL SSGLGDLSIH SLPHAIEEVP HVEDPGINIP DQTVIKKGPV 190 200 210 220 230 240 SLSKSNSNAV SAIPINKDNL FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP 250 260 270 280 290 300 PECLNASLLG GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGEAVHL 310 320 330 340 350 360 ARDFGYVCET EFPAKAVAEF LNRQHSDPNE QVTRKNMLLA TKQICKEFTD LLAQDRSPLG 370 380 390 400 410 420 NSRPNPILEP GIQSCLTHFN LISHGFGSPA VCAAVTALQN YLTEALKAMD KMYLSNNPNS 430 HTDNNAKSSD KEEKHRK
	Isoform 2 [UniParc]. Checksum: 17337CD2D317620F	FASTA	431	47,183
	10 20 30 40 50 60 MLVHSFSAMD RHDGTSNGTA RLPQLGTVGQ SPYTSAPPLS HTPNADFQPP YFPPPYQPIY 70 80 90 100 110 120 PQSQDPYSHV NDPYSLNPLH AQPQPQHPGW PGQRQSQESG LLHTHRGLPH QLSGLDPRRD 130 140 150 160 170 180 YRRHEDLLHG PHALSSGLGD LSIHSLPHAI EEVPHVEDPG INIPDQTVIK KGPVSLSKSN 190 200 210 220 230 240 SNAVSAIPIN KDNLFGGVVN PNEVFCSVPG RLSLLSSTSK YKVTVAEVQR RLSPPECLNA 250 260 270 280 290 300 SLLGGVLRRA KSKNGGRSLR EKLDKIGLNL PAGRRKAANV TLLTSLVEGE AVHLARDFGY 310 320 330 340 350 360 VCETEFPAKA VAEFLNRQHS DPNEQVTRKN MLLATKQICK EFTDLLAQDR SPLGNSRPNP 370 380 390 400 410 420 ILEPGIQSCL THFNLISHGF GSPAVCAAVT ALQNYLTEAL KAMDKMYLSN NPNSHTDNNA 430 KSSDKEEKHR K
	Isoform 4 (AP-2B) [UniParc]. Checksum: C0D74B07799B98A5	FASTA	365	40,557
	10 20 30 40 50 60 MLWKLTDNIK YEDCEDRHDG TSNGTARLPQ LGTVGQSPYT SAPPLSHTPN ADFQPPYFPP 70 80 90 100 110 120 PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR QSQESGLLHT HRGLPHQLSG 130 140 150 160 170 180 LDPRRDYRRH EDLLHGPHAL SSGLGDLSIH SLPHAIEEVP HVEDPGINIP DQTVIKKGPV 190 200 210 220 230 240 SLSKSNSNAV SAIPINKDNL FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP 250 260 270 280 290 300 PECLNASLLG GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGKRIHL 310 320 330 340 350 360 LTRRNFLLGK WIIFSGQMFG RILCQLGSFI FAENIARCEW NYFMAKRNIC MYSYTSILLP SFPLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements." Williams T., Admon A., Luescher B., Tjian R. Genes Dev. 2:1557-1569(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"An alternatively spliced mRNA from the AP-2 gene encodes a negative regulator of transcriptional activation by AP-2." Buettner R., Kannan P., Imhof A., Bauer R., Yim S.O., Glockshuber R., Van Dyke M.W., Tainsky M.A. Mol. Cell. Biol. 13:4174-4185(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4). Tissue: Teratocarcinoma.
[3]	"The genomic structure of the human AP-2 transcription factor." Bauer R., Imhof A., Pscherer A., Kopp H., Moser M., Seegers S., Kerscher M., Tainsky M.A., Hofstaedter F., Buettner R. Nucleic Acids Res. 22:1413-1420(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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].
[5]	"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 2). Tissue: Prostate.
[6]	"Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins." Williams T., Tjian R. Science 251:1067-1071(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[7]	"Analysis of the DNA-binding and activation properties of the human transcription factor AP-2." Williams T., Tjian R. Genes Dev. 5:670-682(1991) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[8]	"Transcription factor AP-2 activity is modulated by protein kinase A-mediated phosphorylation." Garcia M.A., Campillos M., Marina A., Valdivieso F., Vazquez J. FEBS Lett. 444:27-31(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-239, PHOSPHORYLATION.
[9]	"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.
[10]	"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.
[11]	"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-10.
[12]	"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: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH CITED2 AND EP300.
[13]	"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis." Rosse C., L'Hoste S., Offner N., Picard A., Camonis J. J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RALBP1.
[14]	"Physical and functional interactions between the Wwox tumor suppressor protein and the AP-2gamma transcription factor." Aqeilan R.I., Palamarchuk A., Weigel R.J., Herrero J.J., Pekarsky Y., Croce C.M. Cancer Res. 64:8256-8261(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWOX, DOMAIN.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"TFAP2A mutations result in branchio-oculo-facial syndrome." Milunsky J.M., Maher T.A., Zhao G., Roberts A.E., Stalker H.J., Zori R.T., Burch M.N., Clemens M., Mulliken J.B., Smith R., Lin A.E. Am. J. Hum. Genet. 82:1171-1177(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BOFS PRO-249; GLY-254; GLY-255 AND GLU-262.
+	Additional computationally mapped references.

Web resources

Wikipedia

Activatin protein 2 entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	M36711 mRNA. Translation: AAA35539.1. M61156 mRNA. Translation: AAA02487.1. X52611 mRNA. Translation: CAA36842.1. X77343 Genomic DNA. Translation: CAB59735.1. AL138885 Genomic DNA. Translation: CAI20064.1. BC017754 mRNA. Translation: AAH17754.1.
IPI	IPI00181288. IPI00472844. IPI00844409.
PIR	A31752.
RefSeq	NP_001027451.1. NM_001032280.2. NP_001035890.1. NM_001042425.1. NP_003211.1. NM_003220.2.
UniGene	Hs.519880.
3D structure databases
ProteinModelPortal	P05549.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05549. 4 interactions.
MINT	MINT-1524309.
STRING	9606.ENSP00000368924.
PTM databases
PhosphoSite	P05549.
Polymorphism databases
DMDM	135302.
Proteomic databases
PaxDb	P05549.
PRIDE	P05549.
Protocols and materials databases
DNASU	7020.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379604; ENSP00000368924; ENSG00000137203. ENST00000379608; ENSP00000368928; ENSG00000137203. ENST00000482890; ENSP00000418541; ENSG00000137203.
GeneID	7020.
KEGG	hsa:7020.
UCSC	uc003myr.3. human. uc003myu.1. human.
Organism-specific databases
CTD	7020.
GeneCards	GC06M010393.
HGNC	HGNC:11742. TFAP2A.
HPA	CAB000326. HPA028850.
MIM	107580. gene. 113620. phenotype.
neXtProt	NX_P05549.
Orphanet	1297. Branchio-oculo-facial syndrome.
PharmGKB	PA36459.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG300693.
HOGENOM	HOG000231737.
HOVERGEN	HBG002455.
InParanoid	P05549.
KO	K09176.
PhylomeDB	P05549.
Enzyme and pathway databases
Pathway_Interaction_DB	caspase_pathway. Caspase cascade in apoptosis.
Gene expression databases
ArrayExpress	P05549.
Bgee	P05549.
CleanEx	HS_TFAP2A.
Genevestigator	P05549.
GermOnline	ENSG00000137203. Homo sapiens.
Family and domain databases
InterPro	IPR004979. TF_AP2. IPR008121. TF_AP2_alpha_N. IPR013854. TF_AP2_C. [Graphical view]
PANTHER	PTHR10812. PTHR10812. 1 hit.
Pfam	PF03299. TF_AP-2. 1 hit. [Graphical view]
PRINTS	PR01749. AP2ATNSCPFCT. PR01748. AP2TNSCPFCT.
ProtoNet	Search...
Other
ChiTaRS	TFAP2A. human.
GenomeRNAi	7020.
NextBio	27423.
PMAP-CutDB	P05549.
SOURCE	Search...

Entry information

Entry name

AP2A_HUMAN

Accession

Primary (citable) accession number: P05549
Secondary accession number(s): Q13777, Q8N1C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 139 of the entry and version 1 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.