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O75449 (KTNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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 By similarity. Ref.5 Ref.6 Ref.9

Catalytic activity

ATP + H2O = ADP + phosphate. HAMAP-Rule MF_03023

Enzyme regulation

ATPase activity is stimulated by microtubules, which promote homooligomerization By similarity. ATP dependent microtubule severing is stimulated by interaction with KATNB1. HAMAP-Rule MF_03023

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. Interacts with dynein and NDEL1 By similarity. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts with KLHL42 (via the kelch domains). Interacts with CUL3; the interaction is enhanced by KLHL42. Ref.5 Ref.9

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Midbody. Cytoplasmcytoskeleton. 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. Ref.1 Ref.5

Domain

The N-terminus is sufficient for interaction with microtubules. However, high affinity binding to microtubules also requires an intact C-terminal domain and ATP, which promotes oligomerization By similarity. HAMAP-Rule MF_03023

Post-translational modification

Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation. HAMAP-Rule MF_03023

Ubiquitinated by the EDVP E3 ligase complex and subsequently targeted to proteasomal degradation. Ubiquitinated by the BCR(KLHL42) E3 ubiquitin ligase complex, leading to its proteasomal degradation. Ref.8

Sequence similarities

Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytoplasmic microtubule organization

Inferred from electronic annotation. Source: Ensembl

microtubule bundle formation

Inferred from electronic annotation. Source: Ensembl

microtubule severing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

mitotic interphase

Inferred from mutant phenotype Ref.5. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

protein localization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cytoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

growth cone

Inferred from electronic annotation. Source: Ensembl

lipid particle

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.8. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

spindle

Inferred from direct assay Ref.8. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.5Ref.8. Source: UniProtKB

   Molecular_functionATP 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: UniProtKB-EC

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Katanin p60 ATPase-containing subunit A1 HAMAP-Rule MF_03023
PRO_0000084594

Regions

Nucleotide binding249 – 2568ATP Potential
Region1 – 185185Interaction with microtubules HAMAP-Rule MF_03023
Region1 – 7575Interaction with dynein and NDEL1 By similarity
Region1 – 2929Interaction with KATNB1 HAMAP-Rule MF_03023

Amino acid modifications

Modified residue421Phosphoserine; by DYRK2 Ref.9
Modified residue1091Phosphoserine; by DYRK2 Ref.9
Modified residue1331Phosphothreonine; by DYRK2 Ref.9
Modified residue1701Phosphoserine Ref.7 Ref.11

Natural variations

Alternative sequence168 – 24376Missing in isoform 2.
VSP_012948
Alternative sequence384 – 3874AKGR → GMRP in isoform 2.
VSP_012949
Alternative sequence388 – 491104Missing in isoform 2.
VSP_012950

Experimental info

Mutagenesis2551K → A: Abolishes ATP dependent microtubule severing activity and localization to spindle poles. Ref.5 Ref.6
Mutagenesis3081D → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-309. Ref.5
Mutagenesis3091E → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-308. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F431594F478491DD

FASTA49155,965
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 9DF635C4E51147C7
Show »

FASTA31135,319

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-255.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal mitosis in mammalian cells."
Cummings C.M., Bentley C.A., Perdue S.A., Baas P.W., Singer J.D.
J. Biol. Chem. 284:11663-11675(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY THE BCR(KLHL42) COMPLEX.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-42; SER-109 AND THR-133 BY DYRK2, FUNCTION AS KATNA1 KINASE, INTERACTION WITH EDVP COMPLEX.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, 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.
CCDSCCDS5217.1. [O75449-1]
CCDS56456.1. [O75449-2]
RefSeqNP_001191005.1. NM_001204076.1. [O75449-2]
NP_008975.1. NM_007044.3. [O75449-1]
XP_005266861.1. XM_005266804.1. [O75449-1]
UniGeneHs.450175.

3D structure databases

ProteinModelPortalO75449.
SMRO75449. Positions 1-72, 166-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116285. 21 interactions.
STRING9606.ENSP00000335106.

PTM databases

PhosphoSiteO75449.

Proteomic databases

MaxQBO75449.
PaxDbO75449.
PRIDEO75449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335643; ENSP00000335180; ENSG00000186625. [O75449-2]
ENST00000335647; ENSP00000335106; ENSG00000186625. [O75449-1]
ENST00000367411; ENSP00000356381; ENSG00000186625. [O75449-1]
GeneID11104.
KEGGhsa:11104.
UCSCuc003qmr.2. human. [O75449-1]
uc003qmt.3. human. [O75449-2]

Organism-specific databases

CTD11104.
GeneCardsGC06M149957.
HGNCHGNC:6216. KATNA1.
HPAHPA036207.
MIM606696. gene.
neXtProtNX_O75449.
PharmGKBPA30017.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000225142.
HOVERGENHBG057074.
InParanoidO75449.
KOK07767.
OMASQYSDPK.
OrthoDBEOG7SFHWZ.
PhylomeDBO75449.
TreeFamTF323170.

Gene expression databases

ArrayExpressO75449.
BgeeO75449.
CleanExHS_KATNA1.
GenevestigatorO75449.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_03023. Katanin_p60_A1.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR028596. KATNA1.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKATNA1. human.
GeneWikiKATNA1.
GenomeRNAi11104.
NextBio42220.
PROO75449.
SOURCESearch...

Entry information

Entry nameKTNA1_HUMAN
AccessionPrimary (citable) accession number: O75449
Secondary accession number(s): E1P5A3 expand/collapse secondary AC list , Q5TFA8, Q5TFA9, Q86VN2, Q9NU52
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM