SKA2_DANRE
ID SKA2_DANRE Reviewed; 226 AA.
AC Q0P426;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Spindle and kinetochore-associated protein 2;
DE AltName: Full=Protein FAM33A;
GN Name=ska2; Synonyms=fam33a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) 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. In the complex, it is
CC required for ska1 localization. Affinity for microtubules is
CC synergistically enhanced in the presence of the ndc-80 complex and may
CC allow the ndc-80 complex to track depolymerizing microtubules.
CC {ECO:0000250|UniProtKB:Q8WVK7}.
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:Q8WVK7}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q8WVK7}. 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. {ECO:0000250|UniProtKB:Q8WVK7}.
CC -!- SIMILARITY: Belongs to the SKA2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI22317.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC122316; AAI22317.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q0P426; -.
DR SMR; Q0P426; -.
DR STRING; 7955.ENSDARP00000010089; -.
DR PaxDb; Q0P426; -.
DR PRIDE; Q0P426; -.
DR ZFIN; ZDB-GENE-041008-202; ska2.
DR eggNOG; ENOG502S6SM; Eukaryota.
DR InParanoid; Q0P426; -.
DR PhylomeDB; Q0P426; -.
DR Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q0P426; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 InterPro; IPR026762; Ska2.
DR InterPro; IPR042091; Ska2_N.
DR PANTHER; PTHR32017; PTHR32017; 1.
DR Pfam; PF16740; SKA2; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Kinetochore; Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..226
FT /note="Spindle and kinetochore-associated protein 2"
FT /id="PRO_0000373895"
SQ SEQUENCE 226 AA; 25296 MW; 66B363FA78B27568 CRC64;
METVDKLEAM FQKAEADIEY VEKRLKFDFM ASAREAGTFE GNPVELLEDL SAIKARHAAL
CAQVEEIAAE QKRSMDSIRA HLDTTVQLVQ QLQNTADVQV PPLTEEEQEA RDALCSSVAA
LNVEAMPTSE PQSQAQSEAQ NVHEDVSEKT FETVPRSVRG NLKLKDLNAL YKQLFEHFSD
KSRGPISTQR MKKLNMKVND SALKTLQHLK LIELDKKGLV SLLAND