SPC24_MOUSE
ID SPC24_MOUSE Reviewed; 201 AA.
AC Q9D083; Q3TIF5; Q8CD13;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Kinetochore protein Spc24;
GN Name=Spc24; Synonyms=Spbc24;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryonic stem cell, and Testis;
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] (ISOFORM 1).
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and 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: Acts as a component of the essential kinetochore-associated
CC NDC80 complex, which is required for chromosome segregation and spindle
CC checkpoint activity. Required for kinetochore integrity and the
CC organization of stable microtubule binding sites in the outer plate of
CC the kinetochore. The NDC80 complex synergistically enhances the
CC affinity of the SKA1 complex for microtubules and may allow the NDC80
CC complex to track depolymerizing microtubules.
CC {ECO:0000250|UniProtKB:Q8NBT2}.
CC -!- SUBUNIT: Component of the NDC80 complex, which consists of NDC80/HEC1,
CC CDCA1, SPBC24 and SPBC25. The NDC80 complex is formed by two
CC subcomplexes composed of NDC80/HEC1-CDCA1 and SPBC24-SPBC25. Each
CC subcomplex is formed by parallel interactions through the coiled-coil
CC domains of individual subunits. Formation of a tetrameric complex is
CC mediated by interactions between the C-terminal regions of both
CC subunits of the NDC80/HEC1-CDCA1 subcomplex and the N-terminal regions
CC of both subunits of the SPBC24-SPBC25 complex. The tetrameric NDC80
CC complex has an elongated rod-like structure with globular domains at
CC either end (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NBT2}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8NBT2}.
CC Note=Localizes to kinetochores from late prophase to anaphase.
CC Localizes specifically to the outer plate of the kinetochore.
CC {ECO:0000250|UniProtKB:Q8NBT2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D083-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D083-2; Sequence=VSP_020516, VSP_020517;
CC Name=3;
CC IsoId=Q9D083-3; Sequence=VSP_020515;
CC -!- SIMILARITY: Belongs to the SPC24 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK011728; BAB27804.1; -; mRNA.
DR EMBL; AK031680; BAC27510.1; -; mRNA.
DR EMBL; AK075950; BAC36077.1; -; mRNA.
DR EMBL; AK153185; BAE31786.1; -; mRNA.
DR EMBL; AK167877; BAE39891.1; -; mRNA.
DR EMBL; BC086683; AAH86683.1; -; mRNA.
DR EMBL; BC116238; AAI16239.1; -; mRNA.
DR CCDS; CCDS40554.1; -. [Q9D083-1]
DR CCDS; CCDS90517.1; -. [Q9D083-2]
DR RefSeq; NP_080558.1; NM_026282.5. [Q9D083-1]
DR AlphaFoldDB; Q9D083; -.
DR SMR; Q9D083; -.
DR ComplexPortal; CPX-551; Ndc80 complex.
DR IntAct; Q9D083; 1.
DR MINT; Q9D083; -.
DR STRING; 10090.ENSMUSP00000096541; -.
DR iPTMnet; Q9D083; -.
DR PhosphoSitePlus; Q9D083; -.
DR EPD; Q9D083; -.
DR MaxQB; Q9D083; -.
DR PaxDb; Q9D083; -.
DR PeptideAtlas; Q9D083; -.
DR PRIDE; Q9D083; -.
DR ProteomicsDB; 263316; -. [Q9D083-1]
DR ProteomicsDB; 263317; -. [Q9D083-2]
DR ProteomicsDB; 263318; -. [Q9D083-3]
DR Antibodypedia; 53808; 76 antibodies from 17 providers.
DR DNASU; 67629; -.
DR Ensembl; ENSMUST00000098942; ENSMUSP00000096541; ENSMUSG00000074476. [Q9D083-1]
DR Ensembl; ENSMUST00000217382; ENSMUSP00000150475; ENSMUSG00000074476. [Q9D083-3]
DR GeneID; 67629; -.
DR KEGG; mmu:67629; -.
DR UCSC; uc009oml.1; mouse. [Q9D083-1]
DR CTD; 147841; -.
DR MGI; MGI:1914879; Spc24.
DR VEuPathDB; HostDB:ENSMUSG00000074476; -.
DR eggNOG; ENOG502S26V; Eukaryota.
DR GeneTree; ENSGT00390000005584; -.
DR HOGENOM; CLU_119584_0_0_1; -.
DR InParanoid; Q9D083; -.
DR OMA; KWEYDTQ; -.
DR OrthoDB; 1602618at2759; -.
DR PhylomeDB; Q9D083; -.
DR TreeFam; TF333217; -.
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; 67629; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Spc24; mouse.
DR PRO; PR:Q9D083; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D083; protein.
DR Bgee; ENSMUSG00000074476; Expressed in manus and 164 other tissues.
DR ExpressionAtlas; Q9D083; baseline and differential.
DR Genevisible; Q9D083; MM.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0031262; C:Ndc80 complex; ISS:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IC:ComplexPortal.
DR InterPro; IPR013252; Ndc80_Spc24.
DR PANTHER; PTHR22142; PTHR22142; 1.
DR Pfam; PF08286; Spc24; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..201
FT /note="Kinetochore protein Spc24"
FT /id="PRO_0000249560"
FT REGION 1..131
FT /note="Interaction with the N-terminus of SPBC25"
FT /evidence="ECO:0000250"
FT REGION 1..69
FT /note="Interaction with the NDC80-CDCA1 subcomplex"
FT /evidence="ECO:0000250"
FT REGION 132..197
FT /note="Interaction with the C-terminus of SPBC25"
FT /evidence="ECO:0000250"
FT COILED 21..132
FT /evidence="ECO:0000255"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBT2"
FT VAR_SEQ 138..201
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020515"
FT VAR_SEQ 138..160
FT /note="YVAHLYHQISKIQWDYECEPGMI -> PPRPHSGPARPLGQCTALAEVHQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020516"
FT VAR_SEQ 161..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020517"
SQ SEQUENCE 201 AA; 23416 MW; 76192EE5B7114B57 CRC64;
MAAFRDMVEV SNWLLSLLGA NRAEAQQRRL LGSYEQMMER LLEMQDGAYR QLRETLAVEE
EVAQSLLELK ECTRQGDTEL QQLEVELQRT SKEDTCVQAR LRQLITELQE LREMEEELQR
QERDVDEDNT VTIPSAVYVA HLYHQISKIQ WDYECEPGMI KGIHHGPTVA QPIHLDSAQL
SPKFISDYLW SLVDTTWEPE P
