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P05549

- AP2A_HUMAN

UniProt

P05549 - AP2A_HUMAN

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Protein

Transcription factor AP-2-alpha

Gene
TFAP2A, AP2TF, TFAP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. core promoter proximal region sequence-specific DNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein dimerization activity Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: UniProtKB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: UniProtKB
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
  10. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
  11. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  12. RNA polymerase II transcription coactivator activity Source: Ensembl
  13. RNA polymerase II transcription corepressor activity Source: Ensembl
  14. sequence-specific DNA binding Source: UniProtKB
  15. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  16. transcription coactivator activity Source: UniProtKB
  17. transcription regulatory region DNA binding Source: UniProtKB
  18. transcription regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  1. anterior neuropore closure Source: Ensembl
  2. basement membrane organization Source: Ensembl
  3. bone morphogenesis Source: UniProtKB
  4. cellular response to iron ion Source: UniProtKB
  5. cornea development in camera-type eye Source: Ensembl
  6. embryonic body morphogenesis Source: Ensembl
  7. embryonic cranial skeleton morphogenesis Source: UniProtKB
  8. embryonic forelimb morphogenesis Source: UniProtKB
  9. embryonic pattern specification Source: Ensembl
  10. epidermis morphogenesis Source: Ensembl
  11. eyelid development in camera-type eye Source: UniProtKB
  12. face morphogenesis Source: Ensembl
  13. forebrain neuron development Source: Ensembl
  14. inner ear morphogenesis Source: UniProtKB
  15. keratinocyte development Source: Ensembl
  16. kidney development Source: UniProtKB
  17. lens induction in camera-type eye Source: Ensembl
  18. metanephric nephron development Source: Ensembl
  19. negative regulation of apoptotic process Source: UniProtKB
  20. negative regulation of cell proliferation Source: UniProtKB
  21. negative regulation of epidermal growth factor receptor signaling pathway Source: Ensembl
  22. negative regulation of neuron apoptotic process Source: Ensembl
  23. negative regulation of reactive oxygen species metabolic process Source: UniProtKB
  24. negative regulation of transcription, DNA-templated Source: UniProtKB
  25. negative regulation of transcription by competitive promoter binding Source: UniProtKB
  26. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  27. neural crest cell development Source: Ensembl
  28. oculomotor nerve formation Source: UniProtKB
  29. optic cup structural organization Source: UniProtKB
  30. optic vesicle morphogenesis Source: UniProtKB
  31. outflow tract morphogenesis Source: Ensembl
  32. palate development Source: UniProtKB
  33. positive regulation of bone mineralization Source: UniProtKB
  34. positive regulation of cell migration Source: Ensembl
  35. positive regulation of gene expression Source: UniProtKB
  36. positive regulation of neuron apoptotic process Source: UniProtKB
  37. positive regulation of tooth mineralization Source: UniProtKB
  38. positive regulation of transcription, DNA-templated Source: UniProtKB
  39. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  40. regulation of cell differentiation Source: UniProtKB
  41. regulation of neuron differentiation Source: Ensembl
  42. retina layer formation Source: UniProtKB
  43. sensory perception of sound Source: UniProtKB
  44. sympathetic nervous system development Source: Ensembl
  45. transcription from RNA polymerase II promoter Source: GOC
  46. trigeminal nerve development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:TFAP2A
Synonyms:AP2TF, TFAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11742. TFAP2A.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytoplasm Source: HPA
  3. Golgi apparatus Source: HPA
  4. intracellular membrane-bounded organelle Source: HPA
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti249 – 2491L → P in BOFS. 1 Publication
VAR_045838
Natural varianti254 – 2541R → G in BOFS. 1 Publication
VAR_045839
Natural varianti255 – 2551R → G in BOFS. 1 Publication
VAR_045840
Natural varianti262 – 2621G → E in BOFS. 1 Publication
VAR_045841

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi239 – 2391S → A: No phosphorylation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi113620. phenotype.
Orphaneti1297. Branchio-oculo-facial syndrome.
PharmGKBiPA36459.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Transcription factor AP-2-alphaPRO_0000184796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki10 – 10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Modified residuei239 – 2391Phosphoserine; by PKA1 Publication

Post-translational modificationi

Sumoylated on Lys-10; which inhibits transcriptional activity Inferred.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05549.
PaxDbiP05549.
PRIDEiP05549.

PTM databases

PhosphoSiteiP05549.

Miscellaneous databases

PMAP-CutDBP05549.

Expressioni

Gene expression databases

ArrayExpressiP05549.
BgeeiP05549.
CleanExiHS_TFAP2A.
GenevestigatoriP05549.

Organism-specific databases

HPAiCAB000326.
HPA028850.
HPA056871.

Interactioni

Subunit structurei

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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EP300Q094727EBI-347351,EBI-447295
NPM1P067486EBI-347351,EBI-78579

Protein-protein interaction databases

BioGridi112878. 33 interactions.
IntActiP05549. 6 interactions.
MINTiMINT-1524309.
STRINGi9606.ENSP00000368924.

Structurei

3D structure databases

ProteinModelPortaliP05549.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 410131H-S-H (helix-span-helix), dimerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 626WW-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi29 – 11789Gln/Pro-rich (transactivation domain)Add
BLAST

Domaini

The WW-binding motif mediates interaction with WWOX By similarity.1 Publication

Sequence similaritiesi

Belongs to the AP-2 family.

Phylogenomic databases

eggNOGiNOG300693.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiP05549.
KOiK09176.
PhylomeDBiP05549.
TreeFamiTF313718.

Family and domain databases

InterProiIPR004979. TF_AP2.
IPR008121. TF_AP2_alpha_N.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERiPTHR10812. PTHR10812. 1 hit.
PfamiPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSiPR01749. AP2ATNSCPFCT.
PR01748. AP2TNSCPFCT.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: P05549-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MLWKLTDNIK YEDCEDRHDG TSNGTARLPQ LGTVGQSPYT SAPPLSHTPN    50
ADFQPPYFPP PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR 100
QSQESGLLHT HRGLPHQLSG LDPRRDYRRH EDLLHGPHAL SSGLGDLSIH 150
SLPHAIEEVP HVEDPGINIP DQTVIKKGPV SLSKSNSNAV SAIPINKDNL 200
FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP PECLNASLLG 250
GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGEAVHL 300
ARDFGYVCET EFPAKAVAEF LNRQHSDPNE QVTRKNMLLA TKQICKEFTD 350
LLAQDRSPLG NSRPNPILEP GIQSCLTHFN LISHGFGSPA VCAAVTALQN 400
YLTEALKAMD KMYLSNNPNS HTDNNAKSSD KEEKHRK 437
Length:437
Mass (Da):48,062
Last modified:July 1, 1989 - v1
Checksum:iFB8FA33C3AEED71F
GO
Isoform 2 (identifier: P05549-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:431
Mass (Da):47,183
Checksum:i17337CD2D317620F
GO
Isoform 4 (identifier: P05549-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:365
Mass (Da):40,557
Checksum:iC0D74B07799B98A5
GO
Isoform 5 (identifier: P05549-6) [UniParc]FASTAAdd to Basket

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

Note: Gene prediction based on EST data.

Show »
Length:433
Mass (Da):47,440
Checksum:i2521AB97F25AD8B1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti249 – 2491L → P in BOFS. 1 Publication
VAR_045838
Natural varianti254 – 2541R → G in BOFS. 1 Publication
VAR_045839
Natural varianti255 – 2551R → G in BOFS. 1 Publication
VAR_045840
Natural varianti262 – 2621G → E in BOFS. 1 Publication
VAR_045841

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MLWKL…YEDCE → MLVHSFSAM in isoform 2. VSP_043268Add
BLAST
Alternative sequencei1 – 1515MLWKL…YEDCE → MSILAKMGDWQ in isoform 5. VSP_047050Add
BLAST
Alternative sequencei296 – 437142EAVHL…EKHRK → KRIHLLTRRNFLLGKWIIFS GQMFGRILCQLGSFIFAENI ARCEWNYFMAKRNICMYSYT SILLPSFPLP in isoform 4. VSP_006401Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34337.1. [P05549-5]
CCDS43422.1. [P05549-6]
CCDS4510.1. [P05549-1]
PIRiA31752.
RefSeqiNP_001027451.1. NM_001032280.2. [P05549-5]
NP_001035890.1. NM_001042425.1. [P05549-6]
NP_003211.1. NM_003220.2. [P05549-1]
UniGeneiHs.519880.

Genome annotation databases

EnsembliENST00000319516; ENSP00000316516; ENSG00000137203. [P05549-6]
ENST00000379604; ENSP00000368924; ENSG00000137203. [P05549-1]
ENST00000379608; ENSP00000368928; ENSG00000137203. [P05549-5]
ENST00000482890; ENSP00000418541; ENSG00000137203. [P05549-1]
GeneIDi7020.
KEGGihsa:7020.
UCSCiuc003myq.3. human. [P05549-5]
uc003myr.3. human. [P05549-1]
uc003myt.3. human.
uc003myu.1. human. [P05549-2]

Polymorphism databases

DMDMi135302.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Activatin protein 2 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34337.1. [P05549-5 ]
CCDS43422.1. [P05549-6 ]
CCDS4510.1. [P05549-1 ]
PIRi A31752.
RefSeqi NP_001027451.1. NM_001032280.2. [P05549-5 ]
NP_001035890.1. NM_001042425.1. [P05549-6 ]
NP_003211.1. NM_003220.2. [P05549-1 ]
UniGenei Hs.519880.

3D structure databases

ProteinModelPortali P05549.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112878. 33 interactions.
IntActi P05549. 6 interactions.
MINTi MINT-1524309.
STRINGi 9606.ENSP00000368924.

PTM databases

PhosphoSitei P05549.

Polymorphism databases

DMDMi 135302.

Proteomic databases

MaxQBi P05549.
PaxDbi P05549.
PRIDEi P05549.

Protocols and materials databases

DNASUi 7020.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319516 ; ENSP00000316516 ; ENSG00000137203 . [P05549-6 ]
ENST00000379604 ; ENSP00000368924 ; ENSG00000137203 . [P05549-1 ]
ENST00000379608 ; ENSP00000368928 ; ENSG00000137203 . [P05549-5 ]
ENST00000482890 ; ENSP00000418541 ; ENSG00000137203 . [P05549-1 ]
GeneIDi 7020.
KEGGi hsa:7020.
UCSCi uc003myq.3. human. [P05549-5 ]
uc003myr.3. human. [P05549-1 ]
uc003myt.3. human.
uc003myu.1. human. [P05549-2 ]

Organism-specific databases

CTDi 7020.
GeneCardsi GC06M010393.
GeneReviewsi TFAP2A.
HGNCi HGNC:11742. TFAP2A.
HPAi CAB000326.
HPA028850.
HPA056871.
MIMi 107580. gene.
113620. phenotype.
neXtProti NX_P05549.
Orphaneti 1297. Branchio-oculo-facial syndrome.
PharmGKBi PA36459.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300693.
HOGENOMi HOG000231737.
HOVERGENi HBG002455.
InParanoidi P05549.
KOi K09176.
PhylomeDBi P05549.
TreeFami TF313718.

Miscellaneous databases

ChiTaRSi TFAP2A. human.
GeneWikii TFAP2A.
GenomeRNAii 7020.
NextBioi 27423.
PMAP-CutDB P05549.
PROi P05549.
SOURCEi Search...

Gene expression databases

ArrayExpressi P05549.
Bgeei P05549.
CleanExi HS_TFAP2A.
Genevestigatori P05549.

Family and domain databases

InterProi IPR004979. TF_AP2.
IPR008121. TF_AP2_alpha_N.
IPR013854. TF_AP2_C.
[Graphical view ]
PANTHERi PTHR10812. PTHR10812. 1 hit.
Pfami PF03299. TF_AP-2. 1 hit.
[Graphical view ]
PRINTSi PR01749. AP2ATNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: VARIANTS BOFS PRO-249; GLY-254; GLY-255 AND GLU-262.

Entry informationi

Entry nameiAP2A_HUMAN
AccessioniPrimary (citable) accession number: P05549
Secondary accession number(s): Q13777, Q5TAV5, Q8N1C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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