SKA1_XENTR
ID SKA1_XENTR Reviewed; 252 AA.
AC B0BM28;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Spindle and kinetochore-associated protein 1;
GN Name=ska1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the SKA1 complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation. Required for timely anaphase onset during
CC mitosis, when chromosomes undergo bipolar attachment on spindle
CC microtubules leading to silencing of the spindle checkpoint. The SKA1
CC complex is a direct component of the kinetochore-microtubule interface
CC and directly associates with microtubules as oligomeric assemblies. The
CC complex facilitates the processive movement of microspheres along a
CC microtubule in a depolymerization-coupled manner. Affinity for
CC microtubules is synergistically enhanced in the presence of the ndc-80
CC complex and may allow the ndc-80 complex to track depolymerizing
CC microtubules. In the complex, it mediates the interaction with
CC microtubules. {ECO:0000250|UniProtKB:Q96BD8}.
CC -!- SUBUNIT: Component of the SKA1 complex, composed of ska1, ska2 and
CC ska3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q96BD8}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q96BD8}. Note=Localizes to the outer kinetochore
CC and spindle microtubules during mitosis in a NDC80 complex-dependent
CC manner. Localizes to both the mitotic spindle and kinetochore-
CC associated proteins. Associates with kinetochores following microtubule
CC attachment from prometaphase, through mid-anaphase and then vanishes in
CC telophase. {ECO:0000250|UniProtKB:Q96BD8}.
CC -!- SIMILARITY: Belongs to the SKA1 family. {ECO:0000305}.
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DR EMBL; BC158262; AAI58263.1; -; mRNA.
DR RefSeq; NP_001119997.1; NM_001126525.1.
DR AlphaFoldDB; B0BM28; -.
DR SMR; B0BM28; -.
DR STRING; 8364.ENSXETP00000019595; -.
DR PaxDb; B0BM28; -.
DR GeneID; 100144953; -.
DR KEGG; xtr:100144953; -.
DR CTD; 220134; -.
DR Xenbase; XB-GENE-5759531; ska1.
DR eggNOG; KOG4832; Eukaryota.
DR InParanoid; B0BM28; -.
DR OrthoDB; 1354933at2759; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISS:UniProtKB.
DR Gene3D; 1.10.10.1890; -; 1.
DR InterPro; IPR009829; SKA1.
DR InterPro; IPR042031; SKA1-MBD.
DR PANTHER; PTHR28573; PTHR28573; 1.
DR Pfam; PF07160; SKA1; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinetochore; Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..252
FT /note="Spindle and kinetochore-associated protein 1"
FT /id="PRO_0000373888"
FT REGION 84..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..252
FT /note="Microtubule binding"
FT /evidence="ECO:0000250|UniProtKB:Q96BD8"
FT COILED 44..75
FT /evidence="ECO:0000255"
SQ SEQUENCE 252 AA; 28952 MW; BFA0FD14A4EE1389 CRC64;
MDPGDLDELC SHVNSKISLI KKTLQLRNIG QDPSLNSVLS KIAFEMHSLY NLLNNLETEV
QRQETIANSL RELQATVERD FTEASHLKEN IPPHLPKRTQ SSSSAPDEAP EMVVKVAAPE
PAKKPSKEKP IKEMELITVH EFGTVPAYMK NRLTYEQINN IIEELNKAVV GKYKILHQPL
KSLSNQARKQ LSRYKEEETK DTKGQFFIVD QDIKDFTQVK VDKRFHGMLS ILRHCHRLRE
IRGKGLVRYI IC