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P05549

- AP2A_HUMAN

UniProt

P05549 - AP2A_HUMAN

Protein

Transcription factor AP-2-alpha

Gene

TFAP2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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)Curated
    Modified residuei239 – 2391Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Sumoylated on Lys-10; which inhibits transcriptional activity.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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Sequence similaritiesi

    Belongs to the AP-2 family.Curated

    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. 1 PublicationVSP_043268Add
    BLAST
    Alternative sequencei1 – 1515MLWKL…YEDCE → MSILAKMGDWQ in isoform 5. CuratedVSP_047050Add
    BLAST
    Alternative sequencei296 – 437142EAVHL…EKHRK → KRIHLLTRRNFLLGKWIIFS GQMFGRILCQLGSFIFAENI ARCEWNYFMAKRNICMYSYT SILLPSFPLP in isoform 4. 1 PublicationVSP_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

    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: October 1, 2014
    This is version 153 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