Summary: WH2 motif
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WH2 motif Edit Wikipedia article
|Ternary complex of the WH2 domain of mim with actin-dnase I|
The WH2 motif or WH2 domain is an evolutionarily conserved sequence motif contained in proteins. It is found in WASP proteins which control actin polymerisation, therefore, WH2 is important in cellular processes such as cell contractility, cell motility, cell trafficking and cell signalling.
The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is an ~18 amino acids actin-binding motif. This domain was first recognized as an essential element for the regulation of the cytoskeleton by the mammalian Wiskott-Aldrich syndrome protein (WASP) family. WH2 proteins occur in eukaryotes from yeast to mammals, in insect viruses, and in some bacteria. The WH2 domain is found as a modular part of larger proteins; it can be associated with the WH1 or EVH1 domain and with the CRIB domain, and the WH2 domain can occur as a tandem repeat. The WH2 domain binds to actin monomers and can facilitate the assembly of actin monomers into actin filaments.
Human genes encoding proteins containing the WH2 motif include:
- COBL, COBLL1, ESPN, INF2, JMY
- LMOD1, LMOD2, LMOD3
- MTSS1, PXK
- WAS, WASF1, WASF2, WASF3, WASF4, WASL, WASPIP, WHDC1, WIPF1, WIPF2
- PDB 2d1k; Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R (February 2007). "Structural basis for the actin-binding function of missing-in-metastasis". Structure 15 (2): 145–55. doi:10.1016/j.str.2006.12.005. PMC 1853380. PMID 17292833. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1853380/.
- Machesky LM, Insall RH (1998). "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex". Curr. Biol. 8 (25): 1347–56. doi:10.1016/S0960-9822(98)00015-3. PMID 9889097.
- Veltman DM, Insall RH (2010). "WASP family proteins: their evolution and its physiological implications.". Mol Biol Cell 21 (16): 2880–93. doi:10.1091/mbc.E10-04-0372. PMC 2921111. PMID 20573979. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2921111/.
- Machesky LM, Insall RH, Volkman LE (2001). "WASP homology sequences in baculoviruses". Trends Cell Biol. 11 (7): 286–287. doi:10.1016/S0962-8924(01)02009-8. PMID 11434350.
- Lappalainen P, Paunola E, Mattila PK (2002). "WH2 domain: a small, versatile adapter for actin monomers". FEBS Lett. 513 (1): 92–97. doi:10.1016/S0014-5793(01)03242-2. PMID 11911886.
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The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP P42768 and Scar1 (mammalian homologue) to be the region that interacts with actin.
Machesky LM, Insall RH; , Curr Biol 1998;8:1347-1356.: Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. PUBMED:9889097 EPMC:9889097
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003124
The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is an ~18 amino acids actin-binding motif. This domain was first recognised as an essential element for the regulation of the cytoskeleton by the mammalian Wiskott-Aldrich syndrome protein (WASP) family. WH2 proteins occur in eukaryotes from yeast to mammals, in insect viruses, and in some bacteria. The WH2 domain is found as a modular part of larger proteins; it can be associated with the WH1 or EVH1 domain and with the CRIB domain, and the WH2 domain can occur as a tandem repeat. The WH2 domain binds actin monomers and can facilitate the assembly of actin monomers into newly forming actin filaments [PUBMED:11434350, PUBMED:11911886].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||actin binding (GO:0003779)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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Curation and family details
|Seed source:||Alignment kindly provided by SMART|
|Number in seed:||57|
|Number in full:||1560|
|Average length of the domain:||26.60 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||5.24 %|
|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:||15|
|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 WH2 domain has been found. There are 11 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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