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P05549 (AP2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 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-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.10 Ref.13

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. Interacts with KCTD15; this interaction inhibits TFAP2A transcriptional activation. Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18

Subcellular location

Nucleus Ref.13.

Domain

The WW-binding motif mediates interaction with WWOX By similarity. Ref.15

Post-translational modification

Sumoylated on Lys-10; which inhibits transcriptional activity Probable. Ref.12

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.19

Sequence similarities

Belongs to the AP-2 family.

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processanterior neuropore closure

Inferred from electronic annotation. Source: Ensembl

basement membrane organization

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

embryonic body morphogenesis

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

epidermis morphogenesis

Inferred from electronic annotation. Source: Ensembl

eyelid development in camera-type eye

Inferred from sequence or structural similarity. Source: UniProtKB

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

forebrain neuron development

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from mutant phenotype PubMed 21204207. Source: UniProtKB

keratinocyte development

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from mutant phenotype PubMed 21204207. Source: UniProtKB

lens induction in camera-type eye

Inferred from electronic annotation. Source: Ensembl

metanephric nephron development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

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

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20066163Ref.2PubMed 9520389. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 20607706. Source: UniProtKB

neural crest cell development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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: Ensembl

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

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

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11278550PubMed 20808827PubMed 7555706PubMed 7559606. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of cell differentiation

Inferred from direct assay PubMed 20607706. Source: UniProtKB

regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

retina layer formation

Inferred from expression pattern PubMed 20607706. Source: UniProtKB

sensory perception of sound

Inferred from mutant phenotype PubMed 21204207. Source: UniProtKB

sympathetic nervous system development

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21084835PubMed 7555706. Source: GOC

trigeminal nerve development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

centrosome

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.17PubMed 20607706. Source: UniProtKB

   Molecular_functionRNA 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

Inferred from direct assay PubMed 21084835. 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: Ensembl

RNA polymerase II transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 7559606. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10987820PubMed 11447109Ref.10Ref.12Ref.13Ref.17. Source: UniProtKB

protein dimerization activity

Inferred from direct assay Ref.12. Source: UniProtKB

protein homodimerization activity

Traceable author statement PubMed 7559606. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.13Ref.2. Source: UniProtKB

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 7555706. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.13PubMed 7555706Ref.2. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay Ref.13. Source: UniProtKB

transcription regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 18718911. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EP300Q094727EBI-347351,EBI-447295
NPM1P067486EBI-347351,EBI-78579

Alternative products

This entry describes 4 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.
Isoform 5 (identifier: P05549-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MLWKLTDNIKYEDCE → MSILAKMGDWQ
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Transcription factor AP-2-alpha
PRO_0000184796

Regions

Region280 – 410131H-S-H (helix-span-helix), dimerization
Motif57 – 626WW-binding
Compositional bias29 – 11789Gln/Pro-rich (transactivation domain)

Amino acid modifications

Modified residue2391Phosphoserine; by PKA Ref.9
Cross-link10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Natural variations

Alternative sequence1 – 1515MLWKL…YEDCE → MLVHSFSAM in isoform 2.
VSP_043268
Alternative sequence1 – 1515MLWKL…YEDCE → MSILAKMGDWQ in isoform 5.
VSP_047050
Alternative sequence296 – 437142EAVHL…EKHRK → KRIHLLTRRNFLLGKWIIFS GQMFGRILCQLGSFIFAENI ARCEWNYFMAKRNICMYSYT SILLPSFPLP in isoform 4.
VSP_006401
Natural variant2491L → P in BOFS. Ref.19
VAR_045838
Natural variant2541R → G in BOFS. Ref.19
VAR_045839
Natural variant2551R → G in BOFS. Ref.19
VAR_045840
Natural variant2621G → E in BOFS. Ref.19
VAR_045841

Experimental info

Mutagenesis2391S → A: No phosphorylation. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (AP-2A) [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: FB8FA33C3AEED71F

FASTA43748,062
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 17337CD2D317620F
Show »

FASTA43147,183
Isoform 4 (AP-2B) [UniParc].

Checksum: C0D74B07799B98A5
Show »

FASTA36540,557
Isoform 5 [UniParc].

Checksum: 2521AB97F25AD8B1
Show »

FASTA43347,440

References

« Hide '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] (ISOFORM 1), 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. 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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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.
[7]"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.
[8]"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.
[9]"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: PHOSPHORYLATION AT SER-239, MUTAGENESIS OF SER-239.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"Inhibition of neural crest formation by Kctd15 involves regulation of transcription factor AP-2."
Zarelli V.E., Dawid I.B.
Proc. Natl. Acad. Sci. U.S.A. 110:2870-2875(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCTD15.
[19]"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.

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.
CH471087 Genomic DNA. Translation: EAW55249.1.
BC017754 mRNA. Translation: AAH17754.1.
CCDSCCDS34337.1. [P05549-5]
CCDS43422.1. [P05549-6]
CCDS4510.1. [P05549-1]
PIRA31752.
RefSeqNP_001027451.1. NM_001032280.2. [P05549-5]
NP_001035890.1. NM_001042425.1. [P05549-6]
NP_003211.1. NM_003220.2. [P05549-1]
UniGeneHs.519880.

3D structure databases

ProteinModelPortalP05549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112878. 33 interactions.
IntActP05549. 6 interactions.
MINTMINT-1524309.
STRING9606.ENSP00000368924.

PTM databases

PhosphoSiteP05549.

Polymorphism databases

DMDM135302.

Proteomic databases

MaxQBP05549.
PaxDbP05549.
PRIDEP05549.

Protocols and materials databases

DNASU7020.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319516; ENSP00000316516; ENSG00000137203. [P05549-6]
ENST00000379604; ENSP00000368924; ENSG00000137203. [P05549-1]
ENST00000379608; ENSP00000368928; ENSG00000137203. [P05549-5]
ENST00000482890; ENSP00000418541; ENSG00000137203. [P05549-1]
GeneID7020.
KEGGhsa:7020.
UCSCuc003myq.3. human. [P05549-5]
uc003myr.3. human. [P05549-1]
uc003myu.1. human. [P05549-2]

Organism-specific databases

CTD7020.
GeneCardsGC06M010393.
GeneReviewsTFAP2A.
HGNCHGNC:11742. TFAP2A.
HPACAB000326.
HPA028850.
HPA056871.
MIM107580. gene.
113620. phenotype.
neXtProtNX_P05549.
Orphanet1297. Branchio-oculo-facial syndrome.
PharmGKBPA36459.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300693.
HOGENOMHOG000231737.
HOVERGENHBG002455.
InParanoidP05549.
KOK09176.
PhylomeDBP05549.
TreeFamTF313718.

Gene expression databases

ArrayExpressP05549.
BgeeP05549.
CleanExHS_TFAP2A.
GenevestigatorP05549.

Family and domain databases

InterProIPR004979. TF_AP2.
IPR008121. TF_AP2_alpha_N.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERPTHR10812. PTHR10812. 1 hit.
PfamPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSPR01749. AP2ATNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNetSearch...

Other

ChiTaRSTFAP2A. human.
GeneWikiTFAP2A.
GenomeRNAi7020.
NextBio27423.
PMAP-CutDBP05549.
PROP05549.
SOURCESearch...

Entry information

Entry nameAP2A_HUMAN
AccessionPrimary (citable) accession number: P05549
Secondary accession number(s): Q13777, Q5TAV5, Q8N1C6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 151 of the entry and version 1 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