SKA3_MOUSE
ID SKA3_MOUSE Reviewed; 411 AA.
AC Q8C263; Q149T5; Q149T6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Spindle and kinetochore-associated protein 3;
GN Name=Ska3; Synonyms=Rama1;
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=NOD; TISSUE=Dendritic cell;
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 MRNA].
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).
CC -!- FUNCTION: Component of the SKA1 complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation. The SKA1 complex is a direct component of the
CC kinetochore-microtubule interface and directly associates with
CC microtubules as oligomeric assemblies. The complex facilitates the
CC processive movement of microspheres along a microtubule in a
CC depolymerization-coupled manner. In the complex, it mediates the
CC microtubule-stimulated oligomerization. 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:Q8IX90}.
CC -!- SUBUNIT: Component of the SKA1 complex, composed of SKA1, SKA2 and
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 with SKA1; the interaction is direct.
CC {ECO:0000250|UniProtKB:Q8IX90}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q8IX90}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q8IX90}. Note=Localizes to the outer kinetochore
CC and spindle microtubules during mitosis in a NDC80 complex-dependent
CC manner. {ECO:0000250|UniProtKB:Q8IX90}.
CC -!- SIMILARITY: Belongs to the SKA3 family. {ECO:0000305}.
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DR EMBL; AK089223; BAC40798.1; -; mRNA.
DR EMBL; BC117500; AAI17501.1; -; mRNA.
DR EMBL; BC117501; AAI17502.1; -; mRNA.
DR CCDS; CCDS27160.1; -.
DR RefSeq; NP_941007.1; NM_198605.3.
DR AlphaFoldDB; Q8C263; -.
DR SMR; Q8C263; -.
DR BioGRID; 230111; 1.
DR ComplexPortal; CPX-5700; Kinetochore SKA complex.
DR STRING; 10090.ENSMUSP00000022536; -.
DR iPTMnet; Q8C263; -.
DR PhosphoSitePlus; Q8C263; -.
DR REPRODUCTION-2DPAGE; IPI00387253; -.
DR EPD; Q8C263; -.
DR MaxQB; Q8C263; -.
DR PaxDb; Q8C263; -.
DR PeptideAtlas; Q8C263; -.
DR PRIDE; Q8C263; -.
DR ProteomicsDB; 257188; -.
DR Antibodypedia; 22379; 191 antibodies from 27 providers.
DR DNASU; 219114; -.
DR Ensembl; ENSMUST00000022536; ENSMUSP00000022536; ENSMUSG00000021965.
DR GeneID; 219114; -.
DR KEGG; mmu:219114; -.
DR UCSC; uc007udp.1; mouse.
DR CTD; 221150; -.
DR MGI; MGI:3041235; Ska3.
DR VEuPathDB; HostDB:ENSMUSG00000021965; -.
DR eggNOG; ENOG502QSTX; Eukaryota.
DR GeneTree; ENSGT00500000045005; -.
DR HOGENOM; CLU_033334_1_0_1; -.
DR InParanoid; Q8C263; -.
DR OMA; ERYMIPQ; -.
DR OrthoDB; 1070468at2759; -.
DR PhylomeDB; Q8C263; -.
DR TreeFam; TF332721; -.
DR BioGRID-ORCS; 219114; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Ska3; mouse.
DR PRO; PR:Q8C263; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8C263; protein.
DR Bgee; ENSMUSG00000021965; Expressed in embryonic post-anal tail and 121 other tissues.
DR Genevisible; Q8C263; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR033341; SKA3.
DR PANTHER; PTHR48118; PTHR48118; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Kinetochore; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..411
FT /note="Spindle and kinetochore-associated protein 3"
FT /id="PRO_0000089879"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT CONFLICT 391
FT /note="L -> M (in Ref. 2; AAI17501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 45370 MW; 14AE35557A018231 CRC64;
MNPIQSFHCK LRGLATTLDS ETARLLRALD GEDSDFEDSP GRILHDLHSE VQTLKDNVNA
LLDEARLENQ ESTRFKKATK ILMEKNSADV RKLREFFQKY GYQARDKEDS GCEHRVNNST
PELAVCKDIQ KAGVKELSDP CVPSGSVSEE PLRSPQLSDF GLQRYIISQV PANPPQTAAS
LKEERVAETP PAKDPSVQVL KTPRCALRMD DFECETPKLE HFGISEHTMC LNEDYTMGLK
NMKNIKSSLL SGVSGEAIGT GPVTSDNSFA IPGPIIQQME ENDVEYVSSP LPPKFCTPGL
KIPSTMDRTD LVSIDYPLSK PNSSSTDLEI KDCVPLILNS DECYQSFAEP PSSAITSCEN
FATPSPPKVT AIPEDILQMI TKHSSNLASP LDVKVMPRRK GTRGAANKEN W
