ID   SKA2_MOUSE              Reviewed;         120 AA.
AC   Q9CR46; B2KGY1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Spindle and kinetochore-associated protein 2;
DE   AltName: Full=Protein FAM33A;
GN   Name=Ska2; Synonyms=Fam33a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. Forms a heterodimer with SKA1; the heterodimer interacting with
CC       SKA3. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers,
CC       each heterodimer interacting with a molecule of the SKA3 homodimer. The
CC       core SKA1 complex associates with microtubules and forms oligomeric
CC       assemblies. Interacts directly with SKA1. Binds directly to
CC       microtubules; but with a much lower affinity than SKA1 in vivo (By
CC       similarity). {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}.
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DR   EMBL; AK003196; BAB22634.1; -; mRNA.
DR   EMBL; AK013317; BAB28787.1; -; mRNA.
DR   EMBL; AK013370; BAB28814.1; -; mRNA.
DR   EMBL; AK017811; BAB30948.1; -; mRNA.
DR   EMBL; AK162628; BAE36998.1; -; mRNA.
DR   EMBL; AL713917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU468043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466556; EDL15809.1; -; Genomic_DNA.
DR   EMBL; BC117001; AAI17002.1; -; mRNA.
DR   EMBL; BC119167; AAI19168.1; -; mRNA.
DR   CCDS; CCDS25209.1; -.
DR   RefSeq; NP_079653.1; NM_025377.3.
DR   AlphaFoldDB; Q9CR46; -.
DR   SMR; Q9CR46; -.
DR   BioGRID; 211243; 2.
DR   ComplexPortal; CPX-5700; Kinetochore SKA complex.
DR   IntAct; Q9CR46; 1.
DR   STRING; 10090.ENSMUSP00000020794; -.
DR   PhosphoSitePlus; Q9CR46; -.
DR   EPD; Q9CR46; -.
DR   MaxQB; Q9CR46; -.
DR   PaxDb; Q9CR46; -.
DR   PeptideAtlas; Q9CR46; -.
DR   PRIDE; Q9CR46; -.
DR   ProteomicsDB; 261245; -.
DR   Antibodypedia; 31070; 138 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000020794; ENSMUSP00000020794; ENSMUSG00000020492.
DR   GeneID; 66140; -.
DR   KEGG; mmu:66140; -.
DR   UCSC; uc007kti.1; mouse.
DR   CTD; 348235; -.
DR   MGI; MGI:1913390; Ska2.
DR   VEuPathDB; HostDB:ENSMUSG00000020492; -.
DR   eggNOG; ENOG502S6SM; Eukaryota.
DR   GeneTree; ENSGT00390000009588; -.
DR   HOGENOM; CLU_143881_0_0_1; -.
DR   InParanoid; Q9CR46; -.
DR   OMA; MSMEPSA; -.
DR   OrthoDB; 1529470at2759; -.
DR   PhylomeDB; Q9CR46; -.
DR   TreeFam; TF332958; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 66140; 23 hits in 71 CRISPR screens.
DR   ChiTaRS; Ska2; mouse.
DR   PRO; PR:Q9CR46; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9CR46; protein.
DR   Bgee; ENSMUSG00000020492; Expressed in rostral migratory stream and 257 other tissues.
DR   Genevisible; Q9CR46; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000776; C:kinetochore; ISO:MGI.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Kinetochore; Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..120
FT                   /note="Spindle and kinetochore-associated protein 2"
FT                   /id="PRO_0000273161"
SQ   SEQUENCE   120 AA;  13725 MW;  233FE4303B84C117 CRC64;
     MEAEVDKLEL MFQKADSDLD YLQYRLEYEV KTNHPHSAGE KNAVTVLKEL SAIKSRYQAL
     CARFKAVSVE QKETKSCICA TLNKTMTMIQ ELQKQTNLEL TLLTEEEKAA TEPLKSHMPD