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Protein

Transcription factor AP-2-epsilon

Gene

TFAP2E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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-epsilon may play a role in the development of the CNS and in cartilage differentiation (By similarity).By similarity

GO - Molecular functioni

  1. RNA polymerase II regulatory region sequence-specific DNA binding Source: GO_Central
  2. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: GO_Central

GO - Biological processi

  1. anatomical structure development Source: GO_Central
  2. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. regulation of cell proliferation Source: GO_Central
  4. regulation of transcription from RNA polymerase II promoter Source: GO_Central
  5. transcription from RNA polymerase II promoter Source: GOC
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-epsilon
Short name:
AP2-epsilon
Alternative name(s):
Activating enhancer-binding protein 2-epsilon
Gene namesi
Name:TFAP2EImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30774. TFAP2E.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134992283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442Transcription factor AP-2-epsilonPRO_0000309516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461Phosphoserine; by PKABy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6VUC0.
PaxDbiQ6VUC0.
PRIDEiQ6VUC0.

PTM databases

PhosphoSiteiQ6VUC0.

Expressioni

Tissue specificityi

Expressed in skin, primary keratinocytes, immortalized keratinocytes, and HeLa cell line.1 Publication

Gene expression databases

BgeeiQ6VUC0.
CleanExiHS_TFAP2E.
GenevestigatoriQ6VUC0.

Interactioni

Subunit structurei

Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members (By similarity).By similarity

Protein-protein interaction databases

BioGridi130894. 1 interaction.
STRINGi9606.ENSP00000362332.

Structurei

3D structure databases

ProteinModelPortaliQ6VUC0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 417131H-S-H (helix-span-helix), dimerizationSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi54 – 596WW-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 122101Gln/Pro-rich (transactivation domain)Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the AP-2 family.Sequence Analysis

Phylogenomic databases

eggNOGiNOG300693.
GeneTreeiENSGT00550000074577.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiQ6VUC0.
KOiK09179.
OMAiGITNPGE.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ6VUC0.
TreeFamiTF313718.

Family and domain databases

InterProiIPR004979. TF_AP2.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERiPTHR10812. PTHR10812. 1 hit.
PfamiPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSiPR01748. AP2TNSCPFCT.

Sequencei

Sequence statusi: Complete.

Q6VUC0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVHTYSAME RPDGLGAAAG GARLSSLPQA AYGPAPPLCH TPAATAAAEF
60 70 80 90 100
QPPYFPPPYP QPPLPYGQAP DAAAAFPHLA GDPYGGLAPL AQPQPPQAAW
110 120 130 140 150
AAPRAAARAH EEPPGLLAPP ARALGLDPRR DYATAVPRLL HGLADGAHGL
160 170 180 190 200
ADAPLGLPGL AAAPGLEDLQ AMDEPGMSLL DQSVIKKVPI PSKASSLSAL
210 220 230 240 250
SLAKDSLVGG ITNPGEVFCS VPGRLSLLSS TSKYKVTVGE VQRRLSPPEC
260 270 280 290 300
LNASLLGGVL RRAKSKNGGR CLRERLEKIG LNLPAGRRKA ANVTLLTSLV
310 320 330 340 350
EGEAVHLARD FGYVCETEFP AKAAAEYLCR QHADPGELHS RKSMLLAAKQ
360 370 380 390 400
ICKEFADLMA QDRSPLGNSR PALILEPGVQ SCLTHFSLIT HGFGGPAICA
410 420 430 440
ALTAFQNYLL ESLKGLDKMF LSSVGSGHGE TKASEKDAKH RK
Length:442
Mass (Da):46,212
Last modified:July 4, 2004 - v1
Checksum:i823209DA7C0EC527
GO

Sequence cautioni

The sequence AAH41175.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EAX07409.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS393.2.
RefSeqiNP_848643.2. NM_178548.3.
UniGeneiHs.567844.

Genome annotation databases

EnsembliENST00000373235; ENSP00000362332; ENSG00000116819.
GeneIDi339488.
KEGGihsa:339488.
UCSCiuc010ohy.2. human.

Polymorphism databases

DMDMi74749476.

Cross-referencesi

Web resourcesi

Wikipedia

Activatin protein 2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS393.2.
RefSeqiNP_848643.2. NM_178548.3.
UniGeneiHs.567844.

3D structure databases

ProteinModelPortaliQ6VUC0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130894. 1 interaction.
STRINGi9606.ENSP00000362332.

PTM databases

PhosphoSiteiQ6VUC0.

Polymorphism databases

DMDMi74749476.

Proteomic databases

MaxQBiQ6VUC0.
PaxDbiQ6VUC0.
PRIDEiQ6VUC0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373235; ENSP00000362332; ENSG00000116819.
GeneIDi339488.
KEGGihsa:339488.
UCSCiuc010ohy.2. human.

Organism-specific databases

CTDi339488.
GeneCardsiGC01P036038.
HGNCiHGNC:30774. TFAP2E.
MIMi614428. gene.
neXtProtiNX_Q6VUC0.
PharmGKBiPA134992283.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300693.
GeneTreeiENSGT00550000074577.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiQ6VUC0.
KOiK09179.
OMAiGITNPGE.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ6VUC0.
TreeFamiTF313718.

Miscellaneous databases

GenomeRNAii339488.
NextBioi97432.
PROiQ6VUC0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6VUC0.
CleanExiHS_TFAP2E.
GenevestigatoriQ6VUC0.

Family and domain databases

InterProiIPR004979. TF_AP2.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERiPTHR10812. PTHR10812. 1 hit.
PfamiPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSiPR01748. AP2TNSCPFCT.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2002) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: UterusImported.

Entry informationi

Entry nameiAP2E_HUMAN
AccessioniPrimary (citable) accession number: Q6VUC0
Secondary accession number(s): Q8IW12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 12, 2007
Last sequence update: July 4, 2004
Last modified: February 3, 2015
This is version 85 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.