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Q92754

- AP2C_HUMAN

UniProt

Q92754 - AP2C_HUMAN

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Protein
Transcription factor AP-2 gamma
Gene
TFAP2C
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.1 Publication

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: UniProtKB
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
  4. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  5. protein binding Source: UniProtKB
  6. protein dimerization activity Source: UniProtKB
  7. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. cerebral cortex development Source: Ensembl
  3. dichotomous subdivision of terminal units involved in mammary gland duct morphogenesis Source: Ensembl
  4. epithelial cell proliferation involved in mammary gland duct elongation Source: Ensembl
  5. forebrain neuron fate commitment Source: Ensembl
  6. germ-line stem cell maintenance Source: Ensembl
  7. hair follicle development Source: Ensembl
  8. keratinocyte development Source: Ensembl
  9. male gonad development Source: UniProtKB
  10. negative regulation of transcription from RNA polymerase II promoter Source: GOC
  11. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  12. regulation of epidermis development Source: Ensembl
  13. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  14. sebaceous gland development Source: Ensembl
  15. somatic stem cell maintenance Source: Ensembl
  16. trophectodermal cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiQ92754.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TFAP2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11744. TFAP2C.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591Y → A: Loss of interaction with WWOX; when associated with A-64. 1 Publication
Mutagenesisi64 – 641Y → A: Loss of interaction with WWOX; when associated with A-59. 1 Publication

Organism-specific databases

PharmGKBiPA36461.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Transcription factor AP-2 gamma
PRO_0000184803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki10 – 10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei252 – 2521Phosphoserine; by PKA By similarity
Modified residuei434 – 4341Phosphoserine2 Publications

Post-translational modificationi

Sumoylated on Lys-10; which inhibits transcriptional activity.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92754.
PaxDbiQ92754.
PRIDEiQ92754.

PTM databases

PhosphoSiteiQ92754.

Expressioni

Inductioni

During retinoic acid-mediated differentiation.

Gene expression databases

ArrayExpressiQ92754.
BgeeiQ92754.
CleanExiHS_TFAP2C.
GenevestigatoriQ92754.

Organism-specific databases

HPAiCAB016061.
CAB016079.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CITED2Q999672EBI-937309,EBI-937732
UBE2IP632793EBI-937309,EBI-80168

Protein-protein interaction databases

BioGridi112880. 18 interactions.
IntActiQ92754. 7 interactions.
STRINGi9606.ENSP00000201031.

Structurei

3D structure databases

ProteinModelPortaliQ92754.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni293 – 424132H-S-H (helix-span-helix), dimerization
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 646WW-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 11990Gln/Pro-rich (transactivation domain)
Add
BLAST

Domaini

The WW-binding motif mediates interaction with WWOX.1 Publication

Sequence similaritiesi

Belongs to the AP-2 family.

Phylogenomic databases

eggNOGiNOG300693.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiQ92754.
KOiK09177.
OMAiEEVQNVD.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ92754.
TreeFamiTF313718.

Family and domain databases

InterProiIPR004979. TF_AP2.
IPR013854. TF_AP2_C.
IPR008123. TF_AP2_gamma.
[Graphical view]
PANTHERiPTHR10812. PTHR10812. 1 hit.
PfamiPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSiPR01751. AP2CTNSCPFCT.
PR01748. AP2TNSCPFCT.

Sequencei

Sequence statusi: Complete.

Q92754-1 [UniParc]FASTAAdd to Basket

« Hide

MLWKITDNVK YEEDCEDRHD GSSNGNPRVP HLSSAGQHLY SPAPPLSHTG    50
VAEYQPPPYF PPPYQQLAYS QSADPYSHLG EAYAAAINPL HQPAPTGSQQ 100
QAWPGRQSQE GAGLPSHHGR PAGLLPHLSG LEAGAVSARR DAYRRSDLLL 150
PHAHALDAAG LAENLGLHDM PHQMDEVQNV DDQHLLLHDQ TVIRKGPISM 200
TKNPLNLPCQ KELVGAVMNP TEVFCSVPGR LSLLSSTSKY KVTVAEVQRR 250
LSPPECLNAS LLGGVLRRAK SKNGGRSLRE KLDKIGLNLP AGRRKAAHVT 300
LLTSLVEGEA VHLARDFAYV CEAEFPSKPV AEYLTRPHLG GRNEMAARKN 350
MLLAAQQLCK EFTELLSQDR TPHGTSRLAP VLETNIQNCL SHFSLITHGF 400
GSQAICAAVS ALQNYIKEAL IVIDKSYMNP GDQSPADSNK TLEKMEKHRK 450
Length:450
Mass (Da):49,177
Last modified:February 1, 1997 - v1
Checksum:i2D4F5FBC269A34A8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13454.1.
RefSeqiNP_003213.1. NM_003222.3.
UniGeneiHs.473152.

Genome annotation databases

EnsembliENST00000201031; ENSP00000201031; ENSG00000087510.
GeneIDi7022.
KEGGihsa:7022.
UCSCiuc002xya.3. human.

Polymorphism databases

DMDMi12643310.

Cross-referencesi

Web resourcesi

Wikipedia

Activatin protein 2 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13454.1.
RefSeqi NP_003213.1. NM_003222.3.
UniGenei Hs.473152.

3D structure databases

ProteinModelPortali Q92754.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112880. 18 interactions.
IntActi Q92754. 7 interactions.
STRINGi 9606.ENSP00000201031.

PTM databases

PhosphoSitei Q92754.

Polymorphism databases

DMDMi 12643310.

Proteomic databases

MaxQBi Q92754.
PaxDbi Q92754.
PRIDEi Q92754.

Protocols and materials databases

DNASUi 7022.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000201031 ; ENSP00000201031 ; ENSG00000087510 .
GeneIDi 7022.
KEGGi hsa:7022.
UCSCi uc002xya.3. human.

Organism-specific databases

CTDi 7022.
GeneCardsi GC20P055204.
HGNCi HGNC:11744. TFAP2C.
HPAi CAB016061.
CAB016079.
MIMi 601602. gene.
neXtProti NX_Q92754.
PharmGKBi PA36461.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300693.
HOGENOMi HOG000231737.
HOVERGENi HBG002455.
InParanoidi Q92754.
KOi K09177.
OMAi EEVQNVD.
OrthoDBi EOG7HHWS1.
PhylomeDBi Q92754.
TreeFami TF313718.

Enzyme and pathway databases

SignaLinki Q92754.

Miscellaneous databases

GeneWikii TFAP2C.
GenomeRNAii 7022.
NextBioi 27435.
PROi Q92754.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92754.
Bgeei Q92754.
CleanExi HS_TFAP2C.
Genevestigatori Q92754.

Family and domain databases

InterProi IPR004979. TF_AP2.
IPR013854. TF_AP2_C.
IPR008123. TF_AP2_gamma.
[Graphical view ]
PANTHERi PTHR10812. PTHR10812. 1 hit.
Pfami PF03299. TF_AP-2. 1 hit.
[Graphical view ]
PRINTSi PR01751. AP2CTNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].

Entry informationi

Entry nameiAP2C_HUMAN
AccessioniPrimary (citable) accession number: Q92754
Secondary accession number(s): O00685
, O00730, Q86V30, Q8IVB6, Q9P1X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 138 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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