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Q92754 (AP2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor AP-2 gamma

Short name=AP2-gamma
Alternative name(s):
Activating enhancer-binding protein 2 gamma
Transcription factor ERF-1
Gene names
Name:TFAP2C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length450 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. Ref.7

Subunit structure

Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members By similarity. Interacts with WWOX. Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14

Subcellular location

Nucleus Probable.

Induction

During retinoic acid-mediated differentiation.

Domain

The WW-binding motif mediates interaction with WWOX. Ref.11

Post-translational modification

Sumoylated on Lys-10; which inhibits transcriptional activity. Ref.9

Sequence similarities

Belongs to the AP-2 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell signaling

Traceable author statement Ref.2. Source: ProtInc

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

dichotomous subdivision of terminal units involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

epithelial cell proliferation involved in mammary gland duct elongation

Inferred from electronic annotation. Source: Ensembl

forebrain neuron fate commitment

Inferred from electronic annotation. Source: Ensembl

germ-line stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

hair follicle development

Inferred from electronic annotation. Source: Ensembl

keratinocyte development

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from expression pattern PubMed 17848411. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11278550. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 22735262. Source: BHF-UCL

regulation of epidermis development

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

sebaceous gland development

Inferred from electronic annotation. Source: Ensembl

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

trophectodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from direct assay Ref.9. 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 11278550. 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 11278550. Source: UniProtKB

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

protein dimerization activity

Inferred from direct assay Ref.9. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CITED2Q999672EBI-937309,EBI-937732
UBE2IP632793EBI-937309,EBI-80168

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Transcription factor AP-2 gamma
PRO_0000184803

Regions

Region293 – 424132H-S-H (helix-span-helix), dimerization
Motif59 – 646WW-binding
Compositional bias30 – 11990Gln/Pro-rich (transactivation domain)

Amino acid modifications

Modified residue2521Phosphoserine; by PKA By similarity
Modified residue4341Phosphoserine Ref.12 Ref.15
Cross-link10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Experimental info

Mutagenesis591Y → A: Loss of interaction with WWOX; when associated with A-64. Ref.11
Mutagenesis641Y → A: Loss of interaction with WWOX; when associated with A-59. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q92754 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2D4F5FBC269A34A8

FASTA45049,177
        10         20         30         40         50         60 
MLWKITDNVK YEEDCEDRHD GSSNGNPRVP HLSSAGQHLY SPAPPLSHTG VAEYQPPPYF 

        70         80         90        100        110        120 
PPPYQQLAYS QSADPYSHLG EAYAAAINPL HQPAPTGSQQ QAWPGRQSQE GAGLPSHHGR 

       130        140        150        160        170        180 
PAGLLPHLSG LEAGAVSARR DAYRRSDLLL PHAHALDAAG LAENLGLHDM PHQMDEVQNV 

       190        200        210        220        230        240 
DDQHLLLHDQ TVIRKGPISM TKNPLNLPCQ KELVGAVMNP TEVFCSVPGR LSLLSSTSKY 

       250        260        270        280        290        300 
KVTVAEVQRR LSPPECLNAS LLGGVLRRAK SKNGGRSLRE KLDKIGLNLP AGRRKAAHVT 

       310        320        330        340        350        360 
LLTSLVEGEA VHLARDFAYV CEAEFPSKPV AEYLTRPHLG GRNEMAARKN MLLAAQQLCK 

       370        380        390        400        410        420 
EFTELLSQDR TPHGTSRLAP VLETNIQNCL SHFSLITHGF GSQAICAAVS ALQNYIKEAL 

       430        440        450 
IVIDKSYMNP GDQSPADSNK TLEKMEKHRK 

« Hide

References

« Hide 'large scale' references
[1]"Chromosomal mapping of the human and mouse homologues of two new members of the AP-2 family of transcription factors."
Williamson J.A., Bosher J.M., Skinner A., Sheer D., Williams T., Hurst H.C.
Genomics 35:262-264(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary tumor.
[2]"Identification of ERF-1 as a member of the AP2 transcription factor family."
McPherson L.A., Baichwal V.R., Weigel R.J.
Proc. Natl. Acad. Sci. U.S.A. 94:4342-4347(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 203-211 AND 361-370.
Tissue: Mammary tumor.
[3]"Characterisation of the human AP-2gamma and AP-2beta genes."
Haselton M.D., Ibbitt C.J., Hurst H.C.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary and Skin.
[6]"Structure of human AP-2gamma gene."
Nishizawa M., Ito S.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-450.
Tissue: Liver.
[7]"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.
[8]"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.
[9]"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.
[10]"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: INTERACTION WITH CITED2.
[11]"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, MUTAGENESIS OF TYR-59 AND TYR-64.
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Wikipedia

Activatin protein 2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95693 mRNA. Translation: CAA64989.1.
U85658 mRNA. Translation: AAC51305.1.
AJ315934 Genomic DNA. Translation: CAC86997.1.
AL121920 Genomic DNA. Translation: CAC10334.1.
BC035664 mRNA. Translation: AAH35664.2.
BC051829 mRNA. Translation: AAH51829.2.
AB041717 Genomic DNA. Translation: BAC11805.1.
RefSeqNP_003213.1. NM_003222.3.
UniGeneHs.473152.

3D structure databases

ProteinModelPortalQ92754.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112880. 18 interactions.
IntActQ92754. 7 interactions.
STRING9606.ENSP00000201031.

PTM databases

PhosphoSiteQ92754.

Polymorphism databases

DMDM12643310.

Proteomic databases

PaxDbQ92754.
PRIDEQ92754.

Protocols and materials databases

DNASU7022.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000201031; ENSP00000201031; ENSG00000087510.
GeneID7022.
KEGGhsa:7022.
UCSCuc002xya.3. human.

Organism-specific databases

CTD7022.
GeneCardsGC20P055204.
HGNCHGNC:11744. TFAP2C.
HPACAB016061.
CAB016079.
MIM601602. gene.
neXtProtNX_Q92754.
PharmGKBPA36461.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300693.
HOGENOMHOG000231737.
HOVERGENHBG002455.
InParanoidQ92754.
KOK09177.
OMAMAHQMEE.
OrthoDBEOG7HHWS1.
PhylomeDBQ92754.
TreeFamTF313718.

Enzyme and pathway databases

SignaLinkQ92754.

Gene expression databases

ArrayExpressQ92754.
BgeeQ92754.
CleanExHS_TFAP2C.
GenevestigatorQ92754.

Family and domain databases

InterProIPR004979. TF_AP2.
IPR013854. TF_AP2_C.
IPR008123. TF_AP2_gamma.
[Graphical view]
PANTHERPTHR10812. PTHR10812. 1 hit.
PfamPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSPR01751. AP2CTNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNetSearch...

Other

GeneWikiTFAP2C.
GenomeRNAi7022.
NextBio27435.
PROQ92754.
SOURCESearch...

Entry information

Entry nameAP2C_HUMAN
AccessionPrimary (citable) accession number: Q92754
Secondary accession number(s): O00685 expand/collapse secondary AC list , O00730, Q86V30, Q8IVB6, Q9P1X2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 135 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 chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM