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O75449

- KTNA1_HUMAN

UniProt

O75449 - KTNA1_HUMAN

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Protein

Katanin p60 ATPase-containing subunit A1

Gene

KATNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Enzyme regulationi

ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with KATNB1.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi249 – 2568ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microtubule binding Source: UniProtKB
  3. microtubule-severing ATPase activity Source: UniProtKB-EC
  4. protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cytoplasmic microtubule organization Source: Ensembl
  3. microtubule bundle formation Source: Ensembl
  4. microtubule severing Source: UniProtKB-HAMAP
  5. mitotic nuclear division Source: UniProtKB-KW
  6. negative regulation of neuron projection development Source: Ensembl
  7. neuron migration Source: Ensembl
  8. protein localization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Katanin p60 ATPase-containing subunit A1UniRule annotation (EC:3.6.4.3UniRule annotation)
Short name:
Katanin p60 subunit A1UniRule annotation
Alternative name(s):
p60 kataninUniRule annotation
Gene namesi
Name:KATNA1UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6216. KATNA1.

Subcellular locationi

Cytoplasm. Midbody. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome UniRule annotation. Cytoplasmcytoskeletonspindle pole
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.

GO - Cellular componenti

  1. axon Source: Ensembl
  2. centrosome Source: UniProtKB-HAMAP
  3. cytoplasm Source: UniProtKB
  4. growth cone Source: Ensembl
  5. lipid particle Source: Ensembl
  6. microtubule Source: UniProtKB-KW
  7. midbody Source: UniProtKB
  8. neuronal cell body Source: Ensembl
  9. nucleus Source: Ensembl
  10. plasma membrane Source: Ensembl
  11. spindle Source: UniProtKB
  12. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi255 – 2551K → A: Abolishes ATP dependent microtubule severing activity and localization to spindle poles. 2 Publications
Mutagenesisi308 – 3081D → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-309. 1 Publication
Mutagenesisi309 – 3091E → N: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-308. 1 Publication

Organism-specific databases

PharmGKBiPA30017.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Katanin p60 ATPase-containing subunit A1PRO_0000084594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Phosphoserine; by DYRK21 PublicationUniRule annotation
Modified residuei109 – 1091Phosphoserine; by DYRK21 PublicationUniRule annotation
Modified residuei133 – 1331Phosphothreonine; by DYRK21 PublicationUniRule annotation
Modified residuei170 – 1701Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation by DYRK2 triggers ubiquitination and subsequent degradation.4 PublicationsUniRule annotation
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.1 PublicationUniRule annotation

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO75449.
PaxDbiO75449.
PRIDEiO75449.

PTM databases

PhosphoSiteiO75449.

Expressioni

Gene expression databases

BgeeiO75449.
CleanExiHS_KATNA1.
ExpressionAtlasiO75449. baseline and differential.
GenevestigatoriO75449.

Organism-specific databases

HPAiHPA036207.

Interactioni

Subunit structurei

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 KLHL42.2 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi116285. 22 interactions.
STRINGi9606.ENSP00000335106.

Structurei

3D structure databases

ProteinModelPortaliO75449.
SMRiO75449. Positions 1-72, 166-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 185185Interaction with microtubulesAdd
BLAST
Regioni1 – 7575Interaction with dynein and NDEL1By similarityAdd
BLAST
Regioni1 – 2929Interaction with KATNB1Add
BLAST

Domaini

The N-terminus is sufficient for interaction with microtubules, although high affinity binding to microtubules also requires an intact C-terminal domain and ATP, which promotes oligomerization.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00550000074466.
HOGENOMiHOG000225142.
HOVERGENiHBG057074.
InParanoidiO75449.
KOiK07767.
OMAiSQYSDPK.
OrthoDBiEOG7SFHWZ.
PhylomeDBiO75449.
TreeFamiTF323170.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03023. Katanin_p60_A1.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR028596. KATNA1.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75449-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSLLMISENV KLAREYALLG NYDSAMVYYQ GVLDQMNKYL YSVKDTYLQQ
60 70 80 90 100
KWQQVWQEIN VEAKHVKDIM KTLESFKLDS TPLKAAQHDL PASEGEVWSM
110 120 130 140 150
PVPVERRPSP GPRKRQSSQY SDPKSHGNRP STTVRVHRSS AQNVHNDRGK
160 170 180 190 200
AVRCREKKEQ NKGREEKNKS PAAVTEPETN KFDSTGYDKD LVEALERDII
210 220 230 240 250
SQNPNVRWDD IADLVEAKKL LKEAVVLPMW MPEFFKGIRR PWKGVLMVGP
260 270 280 290 300
PGTGKTLLAK AVATECKTTF FNVSSSTLTS KYRGESEKLV RLLFEMARFY
310 320 330 340 350
SPATIFIDEI DSICSRRGTS EEHEASRRVK AELLVQMDGV GGTSENDDPS
360 370 380 390 400
KMVMVLAATN FPWDIDEALR RRLEKRIYIP LPSAKGREEL LRISLRELEL
410 420 430 440 450
ADDVDLASIA ENMEGYSGAD ITNVCRDASL MAMRRRIEGL TPEEIRNLSK
460 470 480 490
EEMHMPTTME DFEMALKKVS KSVSAADIER YEKWIFEFGS C
Length:491
Mass (Da):55,965
Last modified:November 1, 1998 - v1
Checksum:iF431594F478491DD
GO
Isoform 2 (identifier: O75449-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:311
Mass (Da):35,319
Checksum:i9DF635C4E51147C7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei168 – 24376Missing in isoform 2. 1 PublicationVSP_012948Add
BLAST
Alternative sequencei384 – 3874AKGR → GMRP in isoform 2. 1 PublicationVSP_012949
Alternative sequencei388 – 491104Missing in isoform 2. 1 PublicationVSP_012950Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5217.1. [O75449-1]
CCDS56456.1. [O75449-2]
RefSeqiNP_001191005.1. NM_001204076.1. [O75449-2]
NP_008975.1. NM_007044.3. [O75449-1]
XP_005266861.1. XM_005266804.1. [O75449-1]
UniGeneiHs.450175.

Genome annotation databases

EnsembliENST00000335643; ENSP00000335180; ENSG00000186625. [O75449-2]
ENST00000335647; ENSP00000335106; ENSG00000186625. [O75449-1]
ENST00000367411; ENSP00000356381; ENSG00000186625. [O75449-1]
GeneIDi11104.
KEGGihsa:11104.
UCSCiuc003qmr.2. human. [O75449-1]
uc003qmt.3. human. [O75449-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS5217.1. [O75449-1 ]
CCDS56456.1. [O75449-2 ]
RefSeqi NP_001191005.1. NM_001204076.1. [O75449-2 ]
NP_008975.1. NM_007044.3. [O75449-1 ]
XP_005266861.1. XM_005266804.1. [O75449-1 ]
UniGenei Hs.450175.

3D structure databases

ProteinModelPortali O75449.
SMRi O75449. Positions 1-72, 166-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116285. 22 interactions.
STRINGi 9606.ENSP00000335106.

PTM databases

PhosphoSitei O75449.

Proteomic databases

MaxQBi O75449.
PaxDbi O75449.
PRIDEi O75449.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335643 ; ENSP00000335180 ; ENSG00000186625 . [O75449-2 ]
ENST00000335647 ; ENSP00000335106 ; ENSG00000186625 . [O75449-1 ]
ENST00000367411 ; ENSP00000356381 ; ENSG00000186625 . [O75449-1 ]
GeneIDi 11104.
KEGGi hsa:11104.
UCSCi uc003qmr.2. human. [O75449-1 ]
uc003qmt.3. human. [O75449-2 ]

Organism-specific databases

CTDi 11104.
GeneCardsi GC06M149957.
HGNCi HGNC:6216. KATNA1.
HPAi HPA036207.
MIMi 606696. gene.
neXtProti NX_O75449.
PharmGKBi PA30017.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0464.
GeneTreei ENSGT00550000074466.
HOGENOMi HOG000225142.
HOVERGENi HBG057074.
InParanoidi O75449.
KOi K07767.
OMAi SQYSDPK.
OrthoDBi EOG7SFHWZ.
PhylomeDBi O75449.
TreeFami TF323170.

Miscellaneous databases

ChiTaRSi KATNA1. human.
GeneWikii KATNA1.
GenomeRNAii 11104.
NextBioi 42220.
PROi O75449.
SOURCEi Search...

Gene expression databases

Bgeei O75449.
CleanExi HS_KATNA1.
ExpressionAtlasi O75449. baseline and differential.
Genevestigatori O75449.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_03023. Katanin_p60_A1.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR028596. KATNA1.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00674. AAA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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, SUBCELLULAR LOCATION.
  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. 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].

Entry informationi

Entry nameiKTNA1_HUMAN
AccessioniPrimary (citable) accession number: O75449
Secondary accession number(s): E1P5A3
, Q5TFA8, Q5TFA9, Q86VN2, Q9NU52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3