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0  structures 469  species 0  interactions 2812  sequences 22  architectures

Family: TF_AP-2 (PF03299)

Summary: Transcription factor AP-2

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Transcription factor AP-2 Provide feedback

No Pfam abstract.

Literature references

  1. Hilger-Eversheim K, Moser M, Schorle H, Buettner R; , Gene 2000;260:1-12.: Regulatory roles of AP-2 transcription factors in vertebrate development, apoptosis and cell-cycle control. PUBMED:11137286 EPMC:11137286


This tab holds annotation information from the InterPro database.

InterPro entry IPR013854

Activator protein-2 (AP-2) transcription factors constitute a family of closely related and evolutionarily conserved proteins that bind to the DNA consensus sequence GCCNNNGGC and stimulate target gene transcription [ PUBMED:2010091 , PUBMED:1998122 ]. Four different isoforms of AP-2 have been identified in mammals, termed AP-2 alpha, beta, gamma and delta. Each family member shares a common structure, possessing a proline/glutamine-rich domain in the N-terminal region, which is responsible for transcriptional activation [ PUBMED:2010091 ], and a helix-span-helix domain in the C-terminal region, which mediates dimerisation and site-specific DNA binding [ PUBMED:1998122 ].

The AP-2 family have been shown to be critical regulators of gene expression during embryogenesis. They regulate the development of facial prominence and limb buds, and are essential for cranial closure and development of the lens [ PUBMED:11137286 ]; they have also been implicated in tumourigenesis. AP-2 protein expression levels have been found to affect cell transformation, tumour growth and metastasis, and may predict survival in some types of cancer [ PUBMED:9632718 , PUBMED:10864206 ]

This entry represents the C-terminal region of these proteins, including the helix-span-helix domain.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(29)
Full
(2812)
Representative proteomes UniProt
(4716)
RP15
(444)
RP35
(979)
RP55
(2123)
RP75
(2867)
Jalview View  View  View  View  View  View  View 
HTML View  View           
PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(29)
Full
(2812)
Representative proteomes UniProt
(4716)
RP15
(444)
RP35
(979)
RP55
(2123)
RP75
(2867)
Alignment:
Format:
Order:
Sequence:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(29)
Full
(2812)
Representative proteomes UniProt
(4716)
RP15
(444)
RP35
(979)
RP55
(2123)
RP75
(2867)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1736 (release 6.5)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Mifsud W
Number in seed: 29
Number in full: 2812
Average length of the domain: 179.5 aa
Average identity of full alignment: 71 %
Average coverage of the sequence by the domain: 43.73 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.4 23.4
Trusted cut-off 23.4 23.4
Noise cut-off 23.2 23.0
Model length: 197
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044TEL6 View 3D Structure Click here
A0A077Z219 View 3D Structure Click here
A0A077Z3C6 View 3D Structure Click here
A0A0G2KAT2 View 3D Structure Click here
A0A0K0DWA0 View 3D Structure Click here
A0A0K0E4N4 View 3D Structure Click here
A0A0K0ECZ6 View 3D Structure Click here
A0A0K0EEJ1 View 3D Structure Click here
A0A0K0EJI9 View 3D Structure Click here
A0A0N4U5N0 View 3D Structure Click here
A0A0N4U6X0 View 3D Structure Click here
A0A0N4UP43 View 3D Structure Click here
A0A1P6BKK6 View 3D Structure Click here
A0A1P6C2I9 View 3D Structure Click here
A0A286Y8U3 View 3D Structure Click here
A0A2K6VQS0 View 3D Structure Click here
A0A2K6W1X9 View 3D Structure Click here
A0A2R8QRQ5 View 3D Structure Click here
A0A3P7EB32 View 3D Structure Click here
A0A3P7FP95 View 3D Structure Click here
A0A3P7GIJ8 View 3D Structure Click here
A0A3Q0KR56 View 3D Structure Click here
A0A5S6PNR3 View 3D Structure Click here
A0A5S6PYI9 View 3D Structure Click here
A1A4R9 View 3D Structure Click here
D3ZJ69 View 3D Structure Click here
D3ZYF2 View 3D Structure Click here
G2HK15 View 3D Structure Click here
M9PIH9 View 3D Structure Click here
P05549 View 3D Structure Click here
P34056 View 3D Structure Click here
P58197 View 3D Structure Click here
Q09585 View 3D Structure Click here
Q19862 View 3D Structure Click here
Q19863 View 3D Structure Click here
Q4V8P9 View 3D Structure Click here
Q5PQZ4 View 3D Structure Click here
Q5RJ20 View 3D Structure Click here
Q61312 View 3D Structure Click here
Q61313 View 3D Structure Click here

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;