Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor AP-2-alpha

Gene

TFAP2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • bone morphogenesis Source: UniProtKB
  • cellular response to iron ion Source: UniProtKB
  • embryonic cranial skeleton morphogenesis Source: UniProtKB
  • embryonic forelimb morphogenesis Source: UniProtKB
  • eyelid development in camera-type eye Source: UniProtKB
  • inner ear morphogenesis Source: UniProtKB
  • kidney development Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of reactive oxygen species metabolic process Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription by competitive promoter binding Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • oculomotor nerve formation Source: UniProtKB
  • optic cup structural organization Source: UniProtKB
  • optic vesicle morphogenesis Source: UniProtKB
  • palate development Source: UniProtKB
  • positive regulation of bone mineralization Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of neuron apoptotic process Source: UniProtKB
  • positive regulation of tooth mineralization Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of cell differentiation Source: UniProtKB
  • response to lipopolysaccharide Source: Ensembl
  • response to water deprivation Source: Ensembl
  • retina layer formation Source: UniProtKB
  • Schwann cell development Source: Ensembl
  • sensory perception of sound Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: GOC
  • 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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:11742. TFAP2A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Branchiooculofacial syndrome (BOFS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:113620
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.

Polymorphism and mutation databases

BioMutaiTFAP2A.
DMDMi135302.

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

BgeeiP05549.
CleanExiHS_TFAP2A.
ExpressionAtlasiP05549. baseline and differential.
GenevisibleiP05549. HS.

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
GSTO2Q9H4Y53EBI-347351,EBI-10194609
MKRN3Q130643EBI-347351,EBI-2340269
NPM1P067486EBI-347351,EBI-78579
UBE2IP632794EBI-347351,EBI-80168

Protein-protein interaction databases

BioGridi112878. 34 interactions.
IntActiP05549. 80 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.
GeneTreeiENSGT00550000074577.
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. AlignAdd to basket

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

        10         20         30         40         50
MLWKLTDNIK YEDCEDRHDG TSNGTARLPQ LGTVGQSPYT SAPPLSHTPN
60 70 80 90 100
ADFQPPYFPP PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR
110 120 130 140 150
QSQESGLLHT HRGLPHQLSG LDPRRDYRRH EDLLHGPHAL SSGLGDLSIH
160 170 180 190 200
SLPHAIEEVP HVEDPGINIP DQTVIKKGPV SLSKSNSNAV SAIPINKDNL
210 220 230 240 250
FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP PECLNASLLG
260 270 280 290 300
GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGEAVHL
310 320 330 340 350
ARDFGYVCET EFPAKAVAEF LNRQHSDPNE QVTRKNMLLA TKQICKEFTD
360 370 380 390 400
LLAQDRSPLG NSRPNPILEP GIQSCLTHFN LISHGFGSPA VCAAVTALQN
410 420 430
YLTEALKAMD KMYLSNNPNS HTDNNAKSSD KEEKHRK
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000379608; ENSP00000368928; ENSG00000137203. [P05549-5]
ENST00000482890; ENSP00000418541; ENSG00000137203.
GeneIDi7020.
KEGGihsa:7020.
UCSCiuc003myq.3. human. [P05549-5]
uc003myr.3. human. [P05549-1]
uc003myt.3. human.
uc003myu.1. human. [P05549-2]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP05549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112878. 34 interactions.
IntActiP05549. 80 interactions.
MINTiMINT-1524309.
STRINGi9606.ENSP00000368924.

PTM databases

PhosphoSiteiP05549.

Polymorphism and mutation databases

BioMutaiTFAP2A.
DMDMi135302.

Proteomic databases

MaxQBiP05549.
PaxDbiP05549.
PRIDEiP05549.

Protocols and materials databases

DNASUi7020.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7020.
GeneCardsiGC06M010393.
GeneReviewsiTFAP2A.
HGNCiHGNC:11742. TFAP2A.
HPAiCAB000326.
HPA028850.
HPA056871.
MIMi107580. gene.
113620. phenotype.
neXtProtiNX_P05549.
Orphaneti1297. Branchio-oculo-facial syndrome.
PharmGKBiPA36459.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300693.
GeneTreeiENSGT00550000074577.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiP05549.
KOiK09176.
PhylomeDBiP05549.
TreeFamiTF313718.

Miscellaneous databases

ChiTaRSiTFAP2A. human.
GeneWikiiTFAP2A.
GenomeRNAii7020.
NextBioi27423.
PMAP-CutDBP05549.
PROiP05549.
SOURCEiSearch...

Gene expression databases

BgeeiP05549.
CleanExiHS_TFAP2A.
ExpressionAtlasiP05549. baseline and differential.
GenevisibleiP05549. HS.

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.
ProtoNetiSearch...

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: July 22, 2015
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.