ASK1_KLULA
ID ASK1_KLULA Reviewed; 218 AA.
AC Q6CTH8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=DASH complex subunit ASK1;
DE AltName: Full=Associated with spindles and kinetochores protein 1;
DE AltName: Full=Outer kinetochore protein ASK1;
GN Name=ASK1; OrderedLocusNames=KLLA0C12617g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the DASH complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation. The DASH complex mediates the formation and
CC maintenance of bipolar kinetochore-microtubule attachments by forming
CC closed rings around spindle microtubules and establishing interactions
CC with proteins from the central kinetochore (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The DASH complex oligomerizes to form rings that encircle the
CC microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Note=Associates with the mitotic spindle and the
CC kinetochore. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DASH complex ASK1 family. {ECO:0000305}.
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DR EMBL; CR382123; CAH01612.1; -; Genomic_DNA.
DR RefSeq; XP_452761.1; XM_452761.1.
DR AlphaFoldDB; Q6CTH8; -.
DR SMR; Q6CTH8; -.
DR STRING; 28985.XP_452761.1; -.
DR EnsemblFungi; CAH01612; CAH01612; KLLA0_C12617g.
DR GeneID; 2892639; -.
DR KEGG; kla:KLLA0_C12617g; -.
DR eggNOG; ENOG502S2V2; Eukaryota.
DR HOGENOM; CLU_090087_0_0_1; -.
DR InParanoid; Q6CTH8; -.
DR OMA; TIIHFST; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IEA:EnsemblFungi.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:EnsemblFungi.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IEA:EnsemblFungi.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:EnsemblFungi.
DR InterPro; IPR013964; DASH_Ask1.
DR PANTHER; PTHR28200; PTHR28200; 1.
DR Pfam; PF08655; DASH_Ask1; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..218
FT /note="DASH complex subunit ASK1"
FT /id="PRO_0000211315"
FT REGION 109..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 24223 MW; 11F9C25A7E5D22FF CRC64;
MDAVNIEQID QEITLNLQSI DSDLSYCFNK ITKDIIPYVT RYGQTCEDIT NSSSWLKEMF
QQSANVQLVT DQAVESAGQV LEPRTSLFPE VENETDEFHT VDQYPALSQT GVSSAGAPTT
KTGGSVKQDQ FQDQDTDELT QDSAMEKQRK KRKVSLQIHQ HFNSSSSSNS SMENDISANS
SPIKTIPPET ETGTETHNKI QGELAKPGTV IHFNSKRD