Summary: KIX domain
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KIX domain Provide feedback
CBP and P300 bind to the CREB via a domain known as KIX [1]. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun.
Literature references
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Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE; , Cell 1997;91:741-752.: Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. PUBMED:9413984 EPMC:9413984
Internal database links
SCOOP: | KIX_2 |
Similarity to PfamA using HHSearch: | KIX_2 |
External database links
SCOP: | 1kdx |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003101
Transcriptional activators are believed to stimulate gene expression via protein-protein interactions with the basal machinery. The cAMP-regulated transcription factor CREB has been shown to stimulate target gene expression, in part by associating with the coactivator paralogues p300 and CREB binding protein (CBP). CBP and P300 bind to the Ser-133-phosphorylated kinase-inducible domain (KID) of CREB via a region of approximately 90 residues referred to as the KIX domain, which is highly conserved in CBP homologues from Caenorhabditis elegans and Drosophila melanogaster. In addition to CREB, the KIX domain of CBP also recognises the transactivation domains of other nuclear factors, including Myb, Jun, cubitus interruptus, and HTLV-1 virally encoded Tax protein. Thus the KIX domain appears to be a common docking site on CBP for many transcriptional activators. The KIX domain is found in association with other domains, such as the bromodomain, the ZZ-type zinc finger, or the TAZ-type zinc finger [PUBMED:8552098, PUBMED:9413984].
The KIX domain of CBP is composed of three mutually interacting alpha helices, designated alpha1, alpha2 and alpha3, and two short 3(10) helices G1 and G2, that together with the interconnecting loops define a compact structural domain with an extensive hydrophobic core. Helices alpha1 and alpha3 constitute the primary interacting surface for the phosphorylated KID domain (pKID), forming a hydrophobic patch on the protein surface that is large enough to accommodate up to 3 turns of an amphipathic alpha helix, designated alphaB, in pKID. A second alpha helix in pKID, referred to as alphaA, interacts with a different face of the alpha3 helix of KIX. The two helices of pKID are arranged at an angle of about 90 degree and essentially wrap around the alpha3 helix of KIX [PUBMED:8552098, PUBMED:9413984].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | transcription coregulator activity (GO:0003712) |
Biological process | regulation of transcription, DNA-templated (GO:0006355) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan KIX_like (CL0589), which has the following description:
This superfamily is characterised by structures with three helices in a partly opened bundle bundle. There are both creb-binding proteins and activator-binding proteins on mediator subunits, such as higher eukaryotic 13 and fungal 15.
The clan contains the following 2 members:
KIX KIX_2Alignments
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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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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 (5) |
Full (995) |
Representative proteomes | UniProt (1722) |
NCBI (3254) |
Meta (0) |
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RP15 (153) |
RP35 (354) |
RP55 (719) |
RP75 (1030) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (5) |
Full (995) |
Representative proteomes | UniProt (1722) |
NCBI (3254) |
Meta (0) |
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RP15 (153) |
RP35 (354) |
RP55 (719) |
RP75 (1030) |
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Raw Stockholm | |||||||||
Gzipped |
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
Seed source: | Pfam-B_4149 (Release 4.2) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 5 |
Number in full: | 995 |
Average length of the domain: | 79.70 aa |
Average identity of full alignment: | 74 % |
Average coverage of the sequence by the domain: | 3.79 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 81 | ||||||||||||
Family (HMM) version: | 17 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the KIX domain has been found. There are 17 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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