Q6VUC0 (AP2E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor AP-2-epsilon
Short name=AP2-epsilon

Alternative name(s):
Activating enhancer-binding protein 2-epsilon

Gene names

Name:

TFAP2E

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	442 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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. AP-2-epsilon may play a role in the development of the CNS and in cartilage differentiation By similarity. UniProtKB Q6VUP9
Subunit structure	Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members By similarity. UniProtKB P05549 UniProtKB Q6VUP9
Subcellular location	Nucleus By similarity UniProtKB Q6VUP9.
Tissue specificity	Expressed in skin, primary keratinocytes, immortalized keratinocytes, and HeLa cell line. Ref.1
Sequence similarities	Belongs to the AP-2 family.
Sequence caution	The sequence AAH41175.1 differs from that shown. Reason: Erroneous initiation. The sequence EAX07409.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 442	442	Transcription factor AP-2-epsilon		PRO_0000309516
Regions
	Region	287 – 417	131	H-S-H (helix-span-helix), dimerization
	Motif	54 – 59	6	WW-binding
	Compositional bias	22 – 122	101	Gln/Pro-rich (transactivation domain)
Amino acid modifications
	Modified residue	246	1	Phosphoserine; by PKA By similarity UniProtKB P05549

Sequences

	Sequence		Length	Mass (Da)
	Q6VUC0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 823209DA7C0EC527	FASTA	442	46,212
	10 20 30 40 50 60 MLVHTYSAME RPDGLGAAAG GARLSSLPQA AYGPAPPLCH TPAATAAAEF QPPYFPPPYP 70 80 90 100 110 120 QPPLPYGQAP DAAAAFPHLA GDPYGGLAPL AQPQPPQAAW AAPRAAARAH EEPPGLLAPP 130 140 150 160 170 180 ARALGLDPRR DYATAVPRLL HGLADGAHGL ADAPLGLPGL AAAPGLEDLQ AMDEPGMSLL 190 200 210 220 230 240 DQSVIKKVPI PSKASSLSAL SLAKDSLVGG ITNPGEVFCS VPGRLSLLSS TSKYKVTVGE 250 260 270 280 290 300 VQRRLSPPEC LNASLLGGVL RRAKSKNGGR CLRERLEKIG LNLPAGRRKA ANVTLLTSLV 310 320 330 340 350 360 EGEAVHLARD FGYVCETEFP AKAAAEYLCR QHADPGELHS RKSMLLAAKQ ICKEFADLMA 370 380 390 400 410 420 QDRSPLGNSR PALILEPGVQ SCLTHFSLIT HGFGGPAICA ALTAFQNYLL ESLKGLDKMF 430 440 LSSVGSGHGE TKASEKDAKH RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of AP-2 epsilon, a fifth member of the AP-2 family." Tummala R., Romano R.-A., Fuchs E., Sinha S. Gene 321:93-102(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Uterus.
+	Additional computationally mapped references.

Web resources

Wikipedia

Activatin protein 2 entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY326454 mRNA. Translation: AAQ91614.1. AL157951, AC004865 Genomic DNA. Translation: CAI23520.1. CH471059 Genomic DNA. Translation: EAX07409.1. Sequence problems. BC041175 mRNA. Translation: AAH41175.1. Different initiation.
IPI	IPI00237907.
RefSeq	NP_848643.2. NM_178548.3.
UniGene	Hs.567844.
3D structure databases
ProteinModelPortal	Q6VUC0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000362332.
PTM databases
PhosphoSite	Q6VUC0.
Polymorphism databases
DMDM	74749476.
Proteomic databases
PaxDb	Q6VUC0.
PRIDE	Q6VUC0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000373235; ENSP00000362332; ENSG00000116819.
GeneID	339488.
KEGG	hsa:339488.
UCSC	uc010ohy.2. human.
Organism-specific databases
CTD	339488.
GeneCards	GC01P036038.
HGNC	HGNC:30774. TFAP2E.
MIM	614428. gene.
neXtProt	NX_Q6VUC0.
PharmGKB	PA134992283.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG300693.
HOGENOM	HOG000231737.
HOVERGEN	HBG002455.
InParanoid	Q6VUC0.
KO	K09179.
OMA	ARAHEEP.
OrthoDB	EOG466VMB.
Gene expression databases
Bgee	Q6VUC0.
CleanEx	HS_TFAP2E.
Genevestigator	Q6VUC0.
Family and domain databases
InterPro	IPR004979. TF_AP2. IPR013854. TF_AP2_C. [Graphical view]
PANTHER	PTHR10812. PTHR10812. 1 hit.
Pfam	PF03299. TF_AP-2. 1 hit. [Graphical view]
PRINTS	PR01748. AP2TNSCPFCT.
ProtoNet	Search...
Other
GenomeRNAi	339488.
NextBio	97432.
SOURCE	Search...

Entry information

Entry name

AP2E_HUMAN

Accession

Primary (citable) accession number: Q6VUC0
Secondary accession number(s): Q8IW12

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 74 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.