ASK1_YEAS7
ID ASK1_YEAS7 Reviewed; 292 AA.
AC A6ZZR4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
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; ORFNames=SCY_3324;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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. The DASH ring complex may
CC both stabilize microtubules during chromosome attachment in anaphase A,
CC and allow the chromosome to remain attached to the depolymerizing
CC microtubule in anaphase B. Microtubule depolymerization proceeds by
CC protofilament splaying and induces the kinetochore-attached ring to
CC slide longitudinally, thereby helping to transduce depolymerization
CC energy into pulling forces to disjoin chromatids (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The DASH complex is an approximately 210 kDa heterodecamer,
CC which consists of ASK1, DAD1, DAD2, DAD3, DAD4, DAM1, DUO1, HSK3, SPC19
CC and SPC34, with an apparent stoichiometry of one copy of each subunit.
CC DASH oligomerizes into a 50 nm ring composed of about 16 molecules that
CC encircles the microtubule. Integrity of the complex and interactions
CC with central kinetochore proteins are regulated by the spindle assembly
CC checkpoint kinase IPL1 (By similarity). {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; AAFW02000152; EDN59857.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZR4; -.
DR SMR; A6ZZR4; -.
DR PRIDE; A6ZZR4; -.
DR EnsemblFungi; EDN59857; EDN59857; SCY_3324.
DR HOGENOM; CLU_090087_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR InterPro; IPR013964; DASH_Ask1.
DR PANTHER; PTHR28200; PTHR28200; 2.
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 Phosphoprotein.
FT CHAIN 1..292
FT /note="DASH complex subunit ASK1"
FT /id="PRO_0000345954"
FT REGION 99..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 200
FT /note="Phosphoserine; by IPL1"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35734"
FT MOD_RES 250
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000250|UniProtKB:P35734"
SQ SEQUENCE 292 AA; 32046 MW; CB1D3D046857CF1A CRC64;
MDSASKEETL EKLDQEITVN LQKIDSNLSF CFHKITQDII PHVATYSEIC ERIMDSTEWL
GTMFQETGLV NLQANAAAPV GNAPVKSVVS NNVGIFPTSA EEASRESQTD NGPNEADSAV
HVNRDVHSMF TNDSIDDFHT ANITSTGQIL KLPDSSDEDT GSEAVPSREQ TDLTGEGHGG
ADDEQDESTI QRQSRKRKIS LLLQQQYGSS SSMVPSPIVP NKMRKQLAHE EHINNDGDND
DENSNNIESS PLKQGHHHPK GQADDNNEGP DEEESTKEVP KPGTIIHFST NR
