O75449 (KTNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Katanin p60 ATPase-containing subunit A1
Short name=Katanin p60 subunit A1
EC=3.6.4.3

Alternative name(s):
p60 katanin

Gene names

Name:

KATNA1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays, such as during disassembly of interphase microtubules at the G2-M transition. May also be required for microtubule release from the centrosome after nucleation. In mitotic spindles this could allow depolymerization of the microtubule end proximal to the centrosome, and subsequent poleward microtubule flux. In neurons, microtubule release within the cell body may allow their subsequent transport into neuronal processes by microtubule dependent motor proteins. This transport is required for axonal growth By similarity. Ref.5 Ref.6 Ref.10
Catalytic activity	ATP + H2O = ADP + phosphate.
Enzyme regulation	ATPase activity is stimulated by microtubules, which promote homooligomerization By similarity. ATP dependent microtubule severing is stimulated by interaction with KATNB1.
Subunit structure	Can homooligomerize into hexameric rings, which may be promoted by interaction with microtubules By similarity. Interacts with KATNB1, which may serve as a targeting subunit. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Ref.5 Ref.10
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle pole. Note: Predominantly cytoplasmic. Also localized to the interphase centrosome. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1. Ref.1 Ref.5
Domain	The N-terminus is sufficient for interaction with microtubules, although high affinity binding requires an intact C-terminal domain and ATP, which promotes oligomerization By similarity.
Post-translational modification	Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation. Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted to proteasomal degradation.
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW interphase of mitotic cell cycle Inferred from mutant phenotype Ref.5. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	centrosome Inferred from direct assay. Source: HPA microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA spindle pole Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay Ref.5. Source: UniProtKB microtubule-severing ATPase activity Inferred from electronic annotation. Source: EC protein heterodimerization activity Inferred from physical interaction Ref.5. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75449-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O75449-2)

The sequence of this isoform differs from the canonical sequence as follows:
     168-243: Missing.
     384-387: AKGR → GMRP
     388-491: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 491	491	Katanin p60 ATPase-containing subunit A1		PRO_0000084594
Regions
	Nucleotide binding	249 – 256	8	ATP Potential
	Region	1 – 185	185	Interaction with microtubule
	Region	1 – 29	29	Interaction with KATNB1
Amino acid modifications
	Modified residue	42	1	Phosphoserine; by DYRK2 Ref.10
	Modified residue	109	1	Phosphoserine; by DYRK2 Ref.10
	Modified residue	133	1	Phosphothreonine; by DYRK2 Ref.10
	Modified residue	170	1	Phosphoserine Ref.7 Ref.8 Ref.9
Natural variations
	Alternative sequence	168 – 243	76	Missing in isoform 2.		VSP_012948
	Alternative sequence	384 – 387	4	AKGR → GMRP in isoform 2.		VSP_012949
	Alternative sequence	388 – 491	104	Missing in isoform 2.		VSP_012950
Experimental info
	Mutagenesis	255	1	K → A: Abolishes ATP dependent microtubule severing activity and localization to spindle poles. Ref.5 Ref.6
	Mutagenesis	308	1	D → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-309. Ref.5
	Mutagenesis	309	1	E → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-308. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: F431594F478491DD	FASTA	491	55,965
	10 20 30 40 50 60 MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTYLQQ KWQQVWQEIN 70 80 90 100 110 120 VEAKHVKDIM KTLESFKLDS TPLKAAQHDL PASEGEVWSM PVPVERRPSP GPRKRQSSQY 130 140 150 160 170 180 SDPKSHGNRP STTVRVHRSS AQNVHNDRGK AVRCREKKEQ NKGREEKNKS PAAVTEPETN 190 200 210 220 230 240 KFDSTGYDKD LVEALERDII SQNPNVRWDD IADLVEAKKL LKEAVVLPMW MPEFFKGIRR 250 260 270 280 290 300 PWKGVLMVGP PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY 310 320 330 340 350 360 SPATIFIDEI DSICSRRGTS EEHEASRRVK AELLVQMDGV GGTSENDDPS KMVMVLAATN 370 380 390 400 410 420 FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL ADDVDLASIA ENMEGYSGAD 430 440 450 460 470 480 ITNVCRDASL MAMRRRIEGL TPEEIRNLSK EEMHMPTTME DFEMALKKVS KSVSAADIER 490 YEKWIFEFGS C
	Isoform 2 [UniParc]. Checksum: 9DF635C4E51147C7	FASTA	311	35,319
	10 20 30 40 50 60 MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTYLQQ KWQQVWQEIN 70 80 90 100 110 120 VEAKHVKDIM KTLESFKLDS TPLKAAQHDL PASEGEVWSM PVPVERRPSP GPRKRQSSQY 130 140 150 160 170 180 SDPKSHGNRP STTVRVHRSS AQNVHNDRGK AVRCREKKEQ NKGREEKGVL MVGPPGTGKT 190 200 210 220 230 240 LLAKAVATEC KTTFFNVSSS TLTSKYRGES EKLVRLLFEM ARFYSPATIF IDEIDSICSR 250 260 270 280 290 300 RGTSEEHEAS RRVKAELLVQ MDGVGGTSEN DDPSKMVMVL AATNFPWDID EALRRRLEKR 310 IYIPLPSGMR P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Katanin is responsible for the M-phase microtubule-severing activity in Xenopus eggs." McNally F.J., Thomas S. Mol. Biol. Cell 9:1847-1861(1998) [PubMed: 9658175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[5]	"Two domains of p80 katanin regulate microtubule severing and spindle pole targeting by p60 katanin." McNally K.P., Bazirgan O.A., McNally F.J. J. Cell Sci. 113:1623-1633(2000) [PubMed: 10751153] [Abstract] Cited for: FUNCTION, INTERACTION WITH KATNB1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-255; ASP-308 AND GLU-309.
[6]	"Katanin inhibition prevents the redistribution of gamma-tubulin at mitosis." Buster D., McNally K., McNally F.J. J. Cell Sci. 115:1083-1092(2002) [PubMed: 11870226] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-255.
[7]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase." Maddika S., Chen J. Nat. Cell Biol. 11:409-419(2009) [PubMed: 19287380] [Abstract] Cited for: PHOSPHORYLATION AT SER-42; SER-109 AND THR-133 BY DYRK2, FUNCTION AS KATNA1 KINASE, INTERACTION WITH EDVP COMPLEX.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF056022 mRNA. Translation: AAC25114.1. AL078581, BX276089 Genomic DNA. Translation: CAI19504.1. AL078581, BX276089 Genomic DNA. Translation: CAI19505.1. BX276089, AL078581 Genomic DNA. Translation: CAI16431.1. BX276089, AL078581 Genomic DNA. Translation: CAI16432.1. CH471051 Genomic DNA. Translation: EAW47793.1. CH471051 Genomic DNA. Translation: EAW47795.1. BC050428 mRNA. Translation: AAH50428.1.
IPI	IPI00013075. IPI00384339.
RefSeq	NP_001191005.1. NM_001204076.1. NP_008975.1. NM_007044.3.
UniGene	Hs.450175.
3D structure databases
ProteinModelPortal	O75449.
SMR	O75449. Positions 1-72, 190-485.
ModBase	Search...
Protein-protein interaction databases
STRING	O75449.
PTM databases
PhosphoSite	O75449.
Proteomic databases
PRIDE	O75449.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000335647; ENSP00000335106; ENSG00000186625. ENST00000367411; ENSP00000356381; ENSG00000186625.
GeneID	11104.
KEGG	hsa:11104.
UCSC	uc003qmr.1. human. uc003qmt.2. human.
Organism-specific databases
CTD	11104.
GeneCards	GC06M149957.
H-InvDB	HIX0025022.
HGNC	HGNC:6216. KATNA1.
HPA	HPA036207.
MIM	606696. gene.
neXtProt	NX_O75449.
PharmGKB	PA30017.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11205.
GeneTree	ENSGT00550000074466.
HOGENOM	HBG724153.
HOVERGEN	HBG057074.
InParanoid	O75449.
OMA	STTVRVH.
OrthoDB	EOG4CJVGZ.
PhylomeDB	O75449.
Enzyme and pathway databases
Pathway_Interaction_DB	lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
Gene expression databases
ArrayExpress	O75449.
Bgee	O75449.
CleanEx	HS_KATNA1.
Genevestigator	O75449.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR015415. Vps4_C. [Graphical view]
KO	K07767.
Pfam	PF00004. AAA. 1 hit. PF09336. Vps4_C. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	42220.
SOURCE	Search...

Entry information

Entry name

KTNA1_HUMAN

Accession

Primary (citable) accession number: O75449
Secondary accession number(s): E1P5A3 , Q5TFA8, Q5TFA9, Q86VN2, Q9NU52

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.