lisH domain-containing protein ARMC9 isoform 2 [Homo sapiens]
LisH domain-containing protein( domain architecture ID 10652832)
LIS1 homology (LisH) domain-containing protein similar to Homo sapiens LisH domain-containing protein ARMC9 that is required for appropriate acetylation and polyglutamylation of ciliary microtubules, and regulation of cilium length
List of domain hits
Name | Accession | Description | Interval | E-value | ||
LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
7-38 | 5.96e-03 | ||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested 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. : Pssm-ID: 128913 Cd Length: 34 Bit Score: 34.72 E-value: 5.96e-03
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Name | Accession | Description | Interval | E-value | ||
LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
7-38 | 5.96e-03 | ||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested 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. Pssm-ID: 128913 Cd Length: 34 Bit Score: 34.72 E-value: 5.96e-03
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Name | Accession | Description | Interval | E-value | ||
LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
7-38 | 5.96e-03 | ||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested 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. Pssm-ID: 128913 Cd Length: 34 Bit Score: 34.72 E-value: 5.96e-03
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Blast search parameters | ||||
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