KTNA1_HUMAN
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 03-AUG-2022, entry version 180.
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}.
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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; 58.
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; 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; O75449; -.
DR PeptideAtlas; O75449; -.
DR PRIDE; O75449; -.
DR ProteomicsDB; 50017; -. [O75449-1]
DR ProteomicsDB; 50018; -. [O75449-2]
DR Antibodypedia; 33275; 211 antibodies from 25 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 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; YSVRDTY; -.
DR OrthoDB; 717356at2759; -.
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; 16 hits in 1081 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 191 other tissues.
DR ExpressionAtlas; O75449; baseline and differential.
DR Genevisible; O75449; HS.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
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
