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24  structures 1416  species 0  interactions 7043  sequences 156  architectures

Family: LisH (PF08513)

Summary: LisH

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This is the Wikipedia entry entitled "LisH domain". More...

LisH domain Edit Wikipedia article

PDB 1uuj EBI.jpg
n-terminal domain of lissencephaly-1 protein (lis-1)
Symbol LisH
Pfam PF08513
InterPro IPR013720

In molecular biology, the LisH domain (lis homology domain) is a protein domain found in a large number of eukaryotic proteins, from metazoa, fungi and plants that have a wide range of functions. The recently solved structure of the LisH domain in the N-terminal region of LIS1 depicted it as a novel dimerisation motif, and that other structural elements are likely to play an important role in dimerisation.[1][2][3]

The LisH domain is found in the Saccharomyces cerevisiae SIF2 protein, a component of the SET3 complex which is responsible for repressing meiotic genes In SIF2 the LisH domain has been shown to mediate dimer and tetramer formation.[4] It has been shown that the LisH domain helps mediate interaction with components of the SET3 complex.[4]


  1. ^ Kim MH, Cooper DR, Oleksy A, Devedjiev Y, Derewenda U, Reiner O, Otlewski J, Derewenda ZS (June 2004). "The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications". Structure. 12 (6): 987–98. PMID 15274919. doi:10.1016/j.str.2004.03.024. 
  2. ^ Mateja A, Cierpicki T, Paduch M, Derewenda ZS, Otlewski J (March 2006). "The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif". J. Mol. Biol. 357 (2): 621–31. PMID 16445939. doi:10.1016/j.jmb.2006.01.002. 
  3. ^ Gerlitz G, Darhin E, Giorgio G, Franco B, Reiner O (November 2005). "Novel functional features of the Lis-H domain: role in protein dimerization, half-life and cellular localization". Cell Cycle. 4 (11): 1632–40. PMID 16258276. doi:10.4161/cc.4.11.2151. 
  4. ^ a b Cerna D, Wilson DK (2005). "The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex.". J Mol Biol. 351 (4): 923–35. PMID 16051270. doi:10.1016/j.jmb.2005.06.025. 

This article incorporates text from the public domain Pfam and InterPro IPR013720

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

LisH Provide feedback

The LisH (lis homology) domain mediates protein dimerisation and tetramerisation. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex [1].

Literature references

  1. Cerna D, Wilson DK; , J Mol Biol 2005;351:923-935.: The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex. PUBMED:16051270 EPMC:16051270

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006594

The 33-residue LIS1 homology (LisH) motif is found in eukaryotic intracellular proteins involved in microtubule dynamics, cell migration, nucleokinesis and chromosome segregation. The LisH motif is likely to possess a conserved protein-binding function and it has been proposed that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. The LisH motif is found associated to other domains, such as WD-40, SPRY, Kelch, AAA ATPase, RasGEF, or HEAT [ PUBMED:11734546 , PUBMED:12384287 , PUBMED:12559565 , PUBMED:16051270 ].

The secondary structure of the LisH domain is predicted to be two alpha- helices [ PUBMED:11734546 ].

Gene Ontology

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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 LisH (CL0561), which has the following description:

Members of this clan include the LisH dimerisation/tetramerisation domains and the FOP N terminal dimerisation domain.

The clan contains the following 4 members:

FOP_dimer LisH LisH_2 LisH_TPL


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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_8344 (release 17.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Mistry J , Wood V
Number in seed: 50
Number in full: 7043
Average length of the domain: 26.50 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 4.79 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.6 21.6
Trusted cut-off 21.6 21.6
Noise cut-off 21.5 21.5
Model length: 27
Family (HMM) version: 13
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Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 LisH domain has been found. There are 24 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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