ID KTNA1_HUMAN Reviewed; 491 AA. AC O75449; E1P5A3; Q5TFA8; Q5TFA9; Q86VN2; Q9NU52; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 188. DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023}; DE Short=Katanin p60 subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023}; DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03023}; DE AltName: Full=p60 katanin {ECO:0000255|HAMAP-Rule:MF_03023}; GN Name=KATNA1 {ECO:0000255|HAMAP-Rule:MF_03023}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RX PubMed=9658175; DOI=10.1091/mbc.9.7.1847; RA McNally F.J., Thomas S.; RT "Katanin is responsible for the M-phase microtubule-severing activity in RT Xenopus eggs."; RL Mol. Biol. Cell 9:1847-1861(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, INTERACTION WITH KATNB1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP LYS-255; ASP-308 AND GLU-309. RX PubMed=10751153; DOI=10.1242/jcs.113.9.1623; RA McNally K.P., Bazirgan O.A., McNally F.J.; RT "Two domains of p80 katanin regulate microtubule severing and spindle pole RT targeting by p60 katanin."; RL J. Cell Sci. 113:1623-1633(2000). RN [6] RP FUNCTION, AND MUTAGENESIS OF LYS-255. RX PubMed=11870226; DOI=10.1242/jcs.115.5.1083; RA Buster D., McNally K., McNally F.J.; RT "Katanin inhibition prevents the redistribution of gamma-tubulin at RT mitosis."; RL J. Cell Sci. 115:1083-1092(2002). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP UBIQUITINATION BY THE BCR(KLHL42) COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=19261606; DOI=10.1074/jbc.m809374200; RA Cummings C.M., Bentley C.A., Perdue S.A., Baas P.W., Singer J.D.; RT "The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal RT mitosis in mammalian cells."; RL J. Biol. Chem. 284:11663-11675(2009). RN [9] RP PHOSPHORYLATION AT SER-42; SER-109 AND THR-133 BY DYRK2, FUNCTION AS KATNA1 RP KINASE, AND INTERACTION WITH EDVP COMPLEX. RX PubMed=19287380; DOI=10.1038/ncb1848; RA Maddika S., Chen J.; RT "Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 RT ligase."; RL Nat. Cell Biol. 11:409-419(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP INTERACTION WITH CAMSAP2 AND CAMSAP3. RX PubMed=24486153; DOI=10.1016/j.devcel.2014.01.001; RA Jiang K., Hua S., Mohan R., Grigoriev I., Yau K.W., Liu Q., Katrukha E.A., RA Altelaar A.F., Heck A.J., Hoogenraad C.C., Akhmanova A.; RT "Microtubule minus-end stabilization by polymerization-driven CAMSAP RT deposition."; RL Dev. Cell 28:295-309(2014). RN [14] RP INTERACTION WITH CAMSAP3. RX PubMed=28386021; DOI=10.1242/jcs.198010; RA Dong C., Xu H., Zhang R., Tanaka N., Takeichi M., Meng W.; RT "CAMSAP3 accumulates in the pericentrosomal area and accompanies RT microtubule release from the centrosome via katanin."; RL J. Cell Sci. 130:1709-1715(2017). RN [15] RP INTERACTION WITH KATNB1 AND KATNBL1, AND SUBCELLULAR LOCATION. RX PubMed=26929214; DOI=10.1074/mcp.m115.056465; RA Cheung K., Senese S., Kuang J., Bui N., Ongpipattanakul C., Gholkar A., RA Cohn W., Capri J., Whitelegge J.P., Torres J.Z.; RT "Proteomic analysis of the mammalian Katanin family of microtubule-severing RT enzymes defines Katanin p80 subunit B-like 1 (KATNBL1) as a regulator of RT mammalian Katanin microtubule-severing."; RL Mol. Cell. Proteomics 15:1658-1669(2016). CC -!- FUNCTION: Catalytic subunit of a complex which severs microtubules in CC an ATP-dependent manner. Microtubule severing may promote rapid CC reorganization of cellular microtubule arrays and the release of CC microtubules from the centrosome following nucleation. Microtubule CC release from the mitotic spindle poles may allow depolymerization of CC the microtubule end proximal to the spindle pole, leading to poleward CC microtubule flux and poleward motion of chromosome. Microtubule release CC within the cell body of neurons may be required for their transport CC into neuronal processes by microtubule-dependent motor proteins. This CC transport is required for axonal growth. {ECO:0000255|HAMAP- CC Rule:MF_03023, ECO:0000269|PubMed:10751153, CC ECO:0000269|PubMed:11870226, ECO:0000269|PubMed:19287380}. CC -!- CATALYTIC ACTIVITY: CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) CC alpha/beta tubulin heterodimers.; EC=5.6.1.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03023}; CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by microtubules, CC which promote homooligomerization. ATP-dependent microtubule severing CC is stimulated by interaction with KATNB1. {ECO:0000255|HAMAP- CC Rule:MF_03023}. CC -!- SUBUNIT: Can homooligomerize into hexameric rings, which may be CC promoted by interaction with microtubules. Interacts with KATNB1, which CC may serve as a targeting subunit (PubMed:10751153). Interacts with CC ASPM; the katanin complex formation KATNA1:KATNB1 is required for the CC association of ASPM (By similarity). Interacts with dynein and NDEL1. CC Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 CC and DCAF1 proteins (EDVP complex) (PubMed:19287380). Interacts with CC KLHL42 (via the kelch domains). Interacts with CUL3; the interaction is CC enhanced by KLHL42 (PubMed:19261606). Interacts with KATNB1 and KATNBL1 CC (PubMed:26929214). Interacts with CAMSAP2 and CAMSAP3; leading to CC regulate the length of CAMSAP-decorated microtubule stretches CC (PubMed:24486153, PubMed:28386021). {ECO:0000250|UniProtKB:Q9WV86, CC ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:19261606, CC ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:24486153, CC ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:28386021}. CC -!- INTERACTION: CC O75449; Q9BVA0: KATNB1; NbExp=10; IntAct=EBI-1048692, EBI-11147603; CC O75449; Q9H079: KATNBL1; NbExp=10; IntAct=EBI-1048692, EBI-715394; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10751153, CC ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Midbody CC {ECO:0000269|PubMed:19261606}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023}. CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10751153, CC ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Note=Predominantly CC cytoplasmic (PubMed:9658175). Localized diffusely in the cytoplasm CC during the interphase (PubMed:10751153). During metaphase is localized CC throughout the cell and more widely dispersed than the microtubules. In CC anaphase and telophase is localized at the midbody region CC (PubMed:19261606). Also localized to the interphase centrosome and the CC mitotic spindle poles (By similarity). Enhanced recruitment to the CC mitotic spindle poles requires microtubules and interaction with KATNB1 CC (PubMed:10751153). Localizes within the cytoplasm, partially CC overlapping with microtubules, in interphase and to the mitotic spindle CC and spindle poles during mitosis (PubMed:26929214). {ECO:0000255|HAMAP- CC Rule:MF_03023, ECO:0000269|PubMed:10751153, CC ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:26929214, CC ECO:0000269|PubMed:9658175}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75449-1; Sequence=Displayed; CC Name=2; CC IsoId=O75449-2; Sequence=VSP_012948, VSP_012949, VSP_012950; CC -!- DOMAIN: The N-terminus is sufficient for interaction with microtubules, CC although high affinity binding to microtubules also requires an intact CC C-terminal domain and ATP, which promotes oligomerization. CC {ECO:0000255|HAMAP-Rule:MF_03023}. CC -!- PTM: Phosphorylation by DYRK2 triggers ubiquitination and subsequent CC degradation. {ECO:0000255|HAMAP-Rule:MF_03023, CC ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:19287380}. CC -!- PTM: Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, CC leading to its proteasomal degradation. Ubiquitinated by the EDVP E3 CC ligase complex and subsequently targeted for proteasomal degradation. CC {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:19261606}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03023}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF056022; AAC25114.1; -; mRNA. DR EMBL; AL078581; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX276089; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47793.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47795.1; -; Genomic_DNA. DR EMBL; BC050428; AAH50428.1; -; mRNA. DR CCDS; CCDS5217.1; -. [O75449-1] DR CCDS; CCDS56456.1; -. [O75449-2] DR RefSeq; NP_001191005.1; NM_001204076.1. [O75449-2] DR RefSeq; NP_008975.1; NM_007044.3. [O75449-1] DR RefSeq; XP_005266861.1; XM_005266804.2. [O75449-1] DR RefSeq; XP_016865696.1; XM_017010207.1. [O75449-1] DR RefSeq; XP_016865699.1; XM_017010210.1. [O75449-1] DR PDB; 5ZQL; X-ray; 3.01 A; A/B=183-491. DR PDB; 5ZQM; X-ray; 2.90 A; A=183-489. DR PDBsum; 5ZQL; -. DR PDBsum; 5ZQM; -. DR AlphaFoldDB; O75449; -. DR SMR; O75449; -. DR BioGRID; 116285; 67. DR ComplexPortal; CPX-6365; Katanin complex, KATNA1-KATNB1 variant. DR ComplexPortal; CPX-6366; Katanin complex, KATNA1-KATNBL1 variant. DR CORUM; O75449; -. DR IntAct; O75449; 53. DR STRING; 9606.ENSP00000356381; -. DR ChEMBL; CHEMBL3879856; -. DR GlyGen; O75449; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; O75449; -. DR PhosphoSitePlus; O75449; -. DR BioMuta; KATNA1; -. DR EPD; O75449; -. DR jPOST; O75449; -. DR MassIVE; O75449; -. DR MaxQB; O75449; -. DR PaxDb; 9606-ENSP00000356381; -. DR PeptideAtlas; O75449; -. DR ProteomicsDB; 50017; -. [O75449-1] DR ProteomicsDB; 50018; -. [O75449-2] DR Pumba; O75449; -. DR Antibodypedia; 33275; 246 antibodies from 26 providers. DR DNASU; 11104; -. DR Ensembl; ENST00000335643.12; ENSP00000335180.8; ENSG00000186625.14. [O75449-2] DR Ensembl; ENST00000335647.9; ENSP00000335106.5; ENSG00000186625.14. [O75449-1] DR Ensembl; ENST00000367411.7; ENSP00000356381.2; ENSG00000186625.14. [O75449-1] DR GeneID; 11104; -. DR KEGG; hsa:11104; -. DR MANE-Select; ENST00000367411.7; ENSP00000356381.2; NM_007044.4; NP_008975.1. DR UCSC; uc003qmr.3; human. [O75449-1] DR AGR; HGNC:6216; -. DR CTD; 11104; -. DR DisGeNET; 11104; -. DR GeneCards; KATNA1; -. DR HGNC; HGNC:6216; KATNA1. DR HPA; ENSG00000186625; Low tissue specificity. DR MIM; 606696; gene. DR neXtProt; NX_O75449; -. DR OpenTargets; ENSG00000186625; -. DR PharmGKB; PA30017; -. DR VEuPathDB; HostDB:ENSG00000186625; -. DR eggNOG; KOG0738; Eukaryota. DR GeneTree; ENSGT00940000156638; -. DR HOGENOM; CLU_000688_21_1_1; -. DR InParanoid; O75449; -. DR OMA; PRDEMHM; -. DR OrthoDB; 276256at2759; -. DR PhylomeDB; O75449; -. DR TreeFam; TF323170; -. DR BRENDA; 5.6.1.1; 2681. DR PathwayCommons; O75449; -. DR SignaLink; O75449; -. DR SIGNOR; O75449; -. DR BioGRID-ORCS; 11104; 18 hits in 1157 CRISPR screens. DR ChiTaRS; KATNA1; human. DR GeneWiki; KATNA1; -. DR GenomeRNAi; 11104; -. DR Pharos; O75449; Tbio. DR PRO; PR:O75449; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O75449; Protein. DR Bgee; ENSG00000186625; Expressed in sperm and 193 other cell types or tissues. DR ExpressionAtlas; O75449; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0008352; C:katanin complex; IPI:ComplexPortal. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0008568; F:microtubule severing ATPase activity; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:ComplexPortal. DR GO; GO:0051013; P:microtubule severing; IBA:GO_Central. DR CDD; cd21748; Kp60-NTD; 1. DR CDD; cd19522; RecA-like_KTNA1; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1. DR HAMAP; MF_03023; Katanin_p60_A1; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR028596; KATNA1. DR InterPro; IPR048611; KATNA1_MIT. DR InterPro; IPR048612; KTNA1_AAA_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015415; Spast_Vps4_C. DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23074:SF71; KATANIN P60 ATPASE-CONTAINING SUBUNIT A1; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF21126; KATNA1_MIT; 1. DR Pfam; PF09336; Vps4_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00674; AAA; 1. DR Genevisible; O75449; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; KW Cytoplasm; Cytoskeleton; Isomerase; Microtubule; Mitosis; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..491 FT /note="Katanin p60 ATPase-containing subunit A1" FT /id="PRO_0000084594" FT REGION 1..185 FT /note="Interaction with microtubules" FT REGION 1..75 FT /note="Interaction with dynein and NDEL1" FT /evidence="ECO:0000250" FT REGION 1..29 FT /note="Interaction with KATNB1" FT /evidence="ECO:0000269|PubMed:10751153" FT REGION 87..185 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 113..140 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..172 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 249..256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023" FT MOD_RES 42 FT /note="Phosphoserine; by DYRK2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023, FT ECO:0000269|PubMed:19287380" FT MOD_RES 109 FT /note="Phosphoserine; by DYRK2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023, FT ECO:0000269|PubMed:19287380" FT MOD_RES 133 FT /note="Phosphothreonine; by DYRK2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023, FT ECO:0000269|PubMed:19287380" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 168..243 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_012948" FT VAR_SEQ 384..387 FT /note="AKGR -> GMRP (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_012949" FT VAR_SEQ 388..491 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_012950" FT MUTAGEN 255 FT /note="K->A: Abolishes ATP dependent microtubule severing FT activity and localization to spindle poles." FT /evidence="ECO:0000269|PubMed:10751153, FT ECO:0000269|PubMed:11870226" FT MUTAGEN 308 FT /note="D->N: Abolishes ATP dependent microtubule severing FT activity and localization to spindle poles; when associated FT with N-309." FT /evidence="ECO:0000269|PubMed:10751153" FT MUTAGEN 309 FT /note="E->N: Abolishes ATP dependent microtubule severing FT activity and localization to spindle poles; when associated FT with N-308." FT /evidence="ECO:0000269|PubMed:10751153" FT HELIX 189..198 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 200..203 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 215..224 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 226..230 FT /evidence="ECO:0007829|PDB:5ZQM" FT TURN 232..234 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 243..248 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 250..254 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 255..265 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 269..274 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 275..279 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 288..299 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 301..308 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 310..313 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 323..337 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 353..360 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 362..364 FT /evidence="ECO:0007829|PDB:5ZQL" FT HELIX 367..370 FT /evidence="ECO:0007829|PDB:5ZQM" FT STRAND 375..378 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 384..394 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 404..411 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 418..435 FT /evidence="ECO:0007829|PDB:5ZQM" FT TURN 436..439 FT /evidence="ECO:0007829|PDB:5ZQM" FT TURN 443..445 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 459..468 FT /evidence="ECO:0007829|PDB:5ZQM" FT HELIX 475..488 FT /evidence="ECO:0007829|PDB:5ZQM" SQ SEQUENCE 491 AA; 55965 MW; F431594F478491DD CRC64; MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTYLQQ KWQQVWQEIN VEAKHVKDIM KTLESFKLDS TPLKAAQHDL PASEGEVWSM PVPVERRPSP GPRKRQSSQY SDPKSHGNRP STTVRVHRSS AQNVHNDRGK AVRCREKKEQ NKGREEKNKS PAAVTEPETN KFDSTGYDKD LVEALERDII SQNPNVRWDD IADLVEAKKL LKEAVVLPMW MPEFFKGIRR PWKGVLMVGP PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY SPATIFIDEI DSICSRRGTS EEHEASRRVK AELLVQMDGV GGTSENDDPS KMVMVLAATN FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL ADDVDLASIA ENMEGYSGAD ITNVCRDASL MAMRRRIEGL TPEEIRNLSK EEMHMPTTME DFEMALKKVS KSVSAADIER YEKWIFEFGS C //