Q9WV86
uniprot
Q9WV86
canonical
activity_regulation
ACTIVITY REGULATION: ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with KATNB1. {ECO:0000255|HAMAP-Rule:MF_03023}.
uniprot
proteins
amino_acid_sequence
MSLQMIVENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTHLRQKWQQVWQEINVEAKQVKDIMKTLESFKLDITSLQAAQHELPAAEGEVWSLPVPVERRPLPGPRKRQSSQHSDPKPHSNRPSTVVRAHRPSPQNLHNDRGKAVRSREKKEQSKGREEKNKLPAAVTEPEANKFDGTGYDKDLVEALERDIISQNPNVRWYDIADLVEAKKLLQEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRMKAELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVNLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRNLSREAMHMPTTMEDFEMALKKISKSVSAADIERYEKWIVEFGSC
uniprot
proteins
ec_number
5.6.1.1
uniprot
proteins
function
FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. The function in regulating microtubule dynamics at spindle poles seems to depend on the association of the katanin KATNA1:KATNB1 complex with ASPM which recruits it to microtubules. Reversely KATNA1:KATNB1 can enhance ASPM blocking activity on microtubule minus-end growth. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:28436967}.
uniprot
proteins
mass_dalton
55949
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="L->A: Disrupts KATNA1:KATNB1 interaction with ASPM."; /evidence="ECO:0000269|PubMed:28436967"; MUTAGEN 19; /note="L->A: Disrupts KATNA1:KATNB1 interaction with ASPM."; /evidence="ECO:0000269|PubMed:28436967
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation. {ECO:0000255|HAMAP-Rule:MF_03023}.; PTM: Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, leading to its proteasomal degradation. Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted for proteasomal degradation. {ECO:0000255|HAMAP-Rule:MF_03023}.
uniprot
proteins
protein_family
AAA ATPase family
uniprot
proteins
protein_family
Katanin p60 subunit A1 subfamily
uniprot
proteins
pubmed
10445032
uniprot
proteins
pubmed
15215300
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
28436967
uniprot
proteins
sequence_length
491
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}. Midbody {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75449}. Note=Predominantly cytoplasmic. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase and telophase is localized at the midbody region. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (By similarity). {ECO:0000250|UniProtKB:O75449, ECO:0000255|HAMAP-Rule:MF_03023}.
uniprot
proteins