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Protein

Transcription factor AP-2-delta

Gene

TFAP2D

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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-delta
Short name:
AP2-delta
Alternative name(s):
Activating enhancer-binding protein 2-delta
Transcription factor AP-2-beta-like 1
Gene namesi
Name:TFAP2DImported
Synonyms:TFAP2BL11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:15581. TFAP2D.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37984.

Polymorphism and mutation databases

BioMutaiTFAP2D.
DMDMi74750179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Transcription factor AP-2-deltaPRO_0000309513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391Phosphoserine; by PKABy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7Z6R9.
PaxDbiQ7Z6R9.
PRIDEiQ7Z6R9.

PTM databases

PhosphoSiteiQ7Z6R9.

Expressioni

Tissue specificityi

Highly expressed in brain, placenta, skeletal muscle, thymus, small intestine, and prostate, and expressed at lower levels in leukocyte, spleen, testis, ovary and colon. Barely detectable in heart, kidney, liver, lung or pancreas.1 Publication

Gene expression databases

BgeeiQ7Z6R9.
CleanExiHS_TFAP2D.
GenevisibleiQ7Z6R9. HS.

Organism-specific databases

HPAiHPA048962.

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

BioGridi123749. 2 interactions.
STRINGi9606.ENSP00000008391.

Structurei

3D structure databases

ProteinModelPortaliQ7Z6R9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 410131H-S-H (helix-span-helix), dimerizationSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the AP-2 family.Sequence Analysis

Phylogenomic databases

eggNOGiNOG328707.
GeneTreeiENSGT00550000074577.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiQ7Z6R9.
KOiK09178.
OMAiHGEPADF.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ7Z6R9.
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.

Q7Z6R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTFPGLVH DAEIRHDGSN SYRLMQLGCL ESVANSTVAY SSSSPLTYST
60 70 80 90 100
TGTEFASPYF STNHQYTPLH HQSFHYEFQH SHPAVTPDAY SLNSLHHSQQ
110 120 130 140 150
YYQQIHHGEP TDFINLHNAR ALKSSCLDEQ RRELGCLDAY RRHDLSLMSH
160 170 180 190 200
GSQYGMHPDQ RLLPGPSLGL AAAGADDLQG SVEAQCGLVL NGQGGVIRRG
210 220 230 240 250
GTCVVNPTDL FCSVPGRLSL LSSTSKYKVT IAEVKRRLSP PECLNASLLG
260 270 280 290 300
GILRRAKSKN GGRCLREKLD RLGLNLPAGR RKAANVTLLT SLVEGEALHL
310 320 330 340 350
ARDFGYTCET EFPAKAVGEH LARQHMEQKE QTARKKMILA TKQICKEFQD
360 370 380 390 400
LLSQDRSPLG SSRPTPILDL DIQRHLTHFS LITHGFGTPA ICAALSTFQT
410 420 430 440 450
VLSEMLNYLE KHTTHKNGGA ADSGQGHANS EKAPLRKTSE AAVKEGKTEK

TD
Length:452
Mass (Da):49,578
Last modified:October 1, 2003 - v1
Checksum:i6623612B172A59EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161H → Y in AAK16926 (PubMed:11733187).Curated
Sequence conflicti167 – 1671S → N in AAK16926 (PubMed:11733187).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti214 – 2141V → F in a breast cancer sample; somatic mutation. 1 Publication
VAR_036975

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028376 mRNA. Translation: AAK16926.1.
AL031224 Genomic DNA. Translation: CAD92558.1.
CH471081 Genomic DNA. Translation: EAX04354.1.
CCDSiCCDS4933.1.
RefSeqiNP_758438.2. NM_172238.3.
UniGeneiHs.434107.

Genome annotation databases

EnsembliENST00000008391; ENSP00000008391; ENSG00000008197.
GeneIDi83741.
KEGGihsa:83741.
UCSCiuc003paf.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Activatin protein 2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028376 mRNA. Translation: AAK16926.1.
AL031224 Genomic DNA. Translation: CAD92558.1.
CH471081 Genomic DNA. Translation: EAX04354.1.
CCDSiCCDS4933.1.
RefSeqiNP_758438.2. NM_172238.3.
UniGeneiHs.434107.

3D structure databases

ProteinModelPortaliQ7Z6R9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123749. 2 interactions.
STRINGi9606.ENSP00000008391.

PTM databases

PhosphoSiteiQ7Z6R9.

Polymorphism and mutation databases

BioMutaiTFAP2D.
DMDMi74750179.

Proteomic databases

MaxQBiQ7Z6R9.
PaxDbiQ7Z6R9.
PRIDEiQ7Z6R9.

Protocols and materials databases

DNASUi83741.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000008391; ENSP00000008391; ENSG00000008197.
GeneIDi83741.
KEGGihsa:83741.
UCSCiuc003paf.3. human.

Organism-specific databases

CTDi83741.
GeneCardsiGC06P050681.
H-InvDBHIX0032849.
HGNCiHGNC:15581. TFAP2D.
HPAiHPA048962.
MIMi610161. gene.
neXtProtiNX_Q7Z6R9.
PharmGKBiPA37984.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG328707.
GeneTreeiENSGT00550000074577.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiQ7Z6R9.
KOiK09178.
OMAiHGEPADF.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ7Z6R9.
TreeFamiTF313718.

Miscellaneous databases

GenomeRNAii83741.
NextBioi72753.
PROiQ7Z6R9.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z6R9.
CleanExiHS_TFAP2D.
GenevisibleiQ7Z6R9. HS.

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. "Cloning and characterization of a novel human transcription factor AP-2 beta like gene (TFAP2BL1)."
    Cheng C., Ying K., Xu M., Zhao W., Zhou Z., Huang Y., Wang W., Xu J., Zeng L., Xie Y., Mao Y.
    Int. J. Biochem. Cell Biol. 34:78-86(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-214.

Entry informationi

Entry nameiAP2D_HUMAN
AccessioniPrimary (citable) accession number: Q7Z6R9
Secondary accession number(s): Q8IWX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 1, 2003
Last modified: June 24, 2015
This is version 86 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.