Q92754 (AP2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell-cell signaling Traceable author statement. Source: ProtInc male gonad development Inferred from expression pattern. Source: UniProtKB
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from direct assay. 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. Source: UniProtKB protein dimerization activity Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CITED2	Q99967	2	EBI-937309,EBI-937732
UBE2I	P63279	3	EBI-937309,EBI-80168

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 450	450	Transcription factor AP-2 gamma		PRO_0000184803
Regions
	Region	293 – 424	132	H-S-H (helix-span-helix), dimerization
	Motif	59 – 64	6	WW-binding
	Compositional bias	30 – 119	90	Gln/Pro-rich (transactivation domain)
Amino acid modifications
	Modified residue	252	1	Phosphoserine; by PKA By similarity
	Modified residue	434	1	Phosphoserine Ref.12 Ref.13
	Cross-link	10		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Experimental info
	Mutagenesis	59	1	Y → A: Loss of interaction with WWOX; when associated with A-64. Ref.11
	Mutagenesis	64	1	Y → A: Loss of interaction with WWOX; when associated with A-59. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q92754 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 2D4F5FBC269A34A8	FASTA	450	49,177
	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

References

	« Hide 'large scale' referencesShow '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: 8661133] [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: 9113991] [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. , 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: 11780052] [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: 15489334] [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: 11694877] [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: 11744733] [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: 12072434] [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: 12586840] [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: 15548692] [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19115315] [Abstract] Cited for: INTERACTION WITH KCTD1.
+	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.
IPI	IPI00023260.
RefSeq	NP_003213.1. NM_003222.3.
UniGene	Hs.473152.
3D structure databases
ProteinModelPortal	Q92754.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92754. 7 interactions.
STRING	Q92754.
PTM databases
PhosphoSite	Q92754.
Polymorphism databases
DMDM	12643310.
Proteomic databases
PRIDE	Q92754.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000201031; ENSP00000201031; ENSG00000087510.
GeneID	7022.
KEGG	hsa:7022.
UCSC	uc002xya.1. human.
Organism-specific databases
CTD	7022.
GeneCards	GC20P055204.
H-InvDB	HIX0040579.
HGNC	HGNC:11744. TFAP2C.
HPA	CAB016061. CAB016079.
MIM	601602. gene.
neXtProt	NX_Q92754.
PharmGKB	PA36461.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00550000074577.
HOGENOM	HBG506868.
HOVERGEN	HBG002455.
InParanoid	Q92754.
OMA	HQMEEVQ.
OrthoDB	EOG447FT8.
PhylomeDB	Q92754.
Gene expression databases
ArrayExpress	Q92754.
Bgee	Q92754.
CleanEx	HS_TFAP2C.
Genevestigator	Q92754.
GermOnline	ENSG00000087510. Homo sapiens.
Family and domain databases
InterPro	IPR004979. TF_AP2. IPR013854. TF_AP2_C. IPR008123. TF_AP2_gamma. [Graphical view]
KO	K09177.
PANTHER	PTHR10812. TF_AP2. 1 hit.
Pfam	PF03299. TF_AP-2. 1 hit. [Graphical view]
PRINTS	PR01751. AP2CTNSCPFCT. PR01748. AP2TNSCPFCT.
ProtoNet	Search...
Other
NextBio	27435.
SOURCE	Search...

Entry information

Entry name

AP2C_HUMAN

Accession

Primary (citable) accession number: Q92754
Secondary accession number(s): O00685 , O00730, Q86V30, Q8IVB6, Q9P1X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.