Summary: Mitogen-activated protein kinase kinase 1 interacting
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Mitogen-activated protein kinase kinase 1 interacting protein is a small subcellular adaptor protein required for MAPK signaling and ERK1/2 activation. The overall topology of this domain has a central five-stranded beta-sheet sandwiched between a two alpha-helix and a one alpha-helix layer .
Kurzbauer R, Teis D, de Araujo ME, Maurer-Stroh S, Eisenhaber F, Bourenkov GP, Bartunik HD, Hekman M, Rapp UR, Huber LA, Clausen T; , Proc Natl Acad Sci U S A. 2004;101:10984-10989.: Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes. PUBMED:15263099 EPMC:15263099
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015019Ragulator complex protein LAMTOR3 (for lysosomal adaptor and MAPK and MTOR activator 3) is a regulator of the TOR pathway, which is a signalling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids [PUBMED:19539012].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||regulation of TOR signaling cascade (GO:0032006)|
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The families here all show the Profilin-like fold, and represent both the Profilin (actin-binding protein) (55770) and the Roadblock/LC7 domain-type (103196) superfamilies.
The clan contains the following 3 members:MAPKK1_Int Profilin Robl_LC7
We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Author:||Mistry J, Sammut SJ|
|Number in seed:||7|
|Number in full:||141|
|Average length of the domain:||113.10 aa|
|Average identity of full alignment:||45 %|
|Average coverage of the sequence by the domain:||83.01 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 MAPKK1_Int domain has been found. There are 5 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 seqence.
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