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Q6VUC0 (AP2E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor AP-2-epsilon

Short name=AP2-epsilon
Alternative name(s):
Activating enhancer-binding protein 2-epsilon
Gene names
Name:TFAP2E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442Transcription factor AP-2-epsilon
PRO_0000309516

Regions

Region287 – 417131H-S-H (helix-span-helix), dimerization
Motif54 – 596WW-binding
Compositional bias22 – 122101Gln/Pro-rich (transactivation domain)

Amino acid modifications

Modified residue2461Phosphoserine; by PKA By similarity UniProtKB P05549

Sequences

Sequence LengthMass (Da)Tools
Q6VUC0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 823209DA7C0EC527

FASTA44246,212
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS393.2.
RefSeqNP_848643.2. NM_178548.3.
UniGeneHs.567844.

3D structure databases

ProteinModelPortalQ6VUC0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid130894. 1 interaction.
STRING9606.ENSP00000362332.

PTM databases

PhosphoSiteQ6VUC0.

Polymorphism databases

DMDM74749476.

Proteomic databases

MaxQBQ6VUC0.
PaxDbQ6VUC0.
PRIDEQ6VUC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373235; ENSP00000362332; ENSG00000116819.
GeneID339488.
KEGGhsa:339488.
UCSCuc010ohy.2. human.

Organism-specific databases

CTD339488.
GeneCardsGC01P036038.
HGNCHGNC:30774. TFAP2E.
MIM614428. gene.
neXtProtNX_Q6VUC0.
PharmGKBPA134992283.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300693.
HOGENOMHOG000231737.
HOVERGENHBG002455.
InParanoidQ6VUC0.
KOK09179.
OMAGITNPGE.
OrthoDBEOG7HHWS1.
PhylomeDBQ6VUC0.
TreeFamTF313718.

Gene expression databases

BgeeQ6VUC0.
CleanExHS_TFAP2E.
GenevestigatorQ6VUC0.

Family and domain databases

InterProIPR004979. TF_AP2.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERPTHR10812. PTHR10812. 1 hit.
PfamPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSPR01748. AP2TNSCPFCT.
ProtoNetSearch...

Other

GenomeRNAi339488.
NextBio97432.
PROQ6VUC0.
SOURCESearch...

Entry information

Entry nameAP2E_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 81 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 1

Human chromosome 1: entries, gene names and cross-references to MIM