SPC25_MOUSE
ID SPC25_MOUSE Reviewed; 226 AA.
AC Q3UA16; Q9D021; Q9D1K6;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Kinetochore protein Spc25;
GN Name=Spc25; Synonyms=Spbc25;
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, Embryo, and Embryonic liver;
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).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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: 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:Q9HBM1}.
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:Q9HBM1}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9HBM1}.
CC Note=Localizes to kinetochores from late prophase to anaphase.
CC Localizes specifically to the outer plate of the kinetochore.
CC {ECO:0000250|UniProtKB:Q9HBM1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UA16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UA16-2; Sequence=VSP_020518;
CC Name=3;
CC IsoId=Q3UA16-3; Sequence=VSP_020519;
CC -!- SIMILARITY: Belongs to the SPC25 family. {ECO:0000305}.
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DR EMBL; AK003408; BAB22772.1; -; mRNA.
DR EMBL; AK011893; BAB27900.1; -; mRNA.
DR EMBL; AK146727; BAE27390.1; -; mRNA.
DR EMBL; AK151554; BAE30499.1; -; mRNA.
DR EMBL; BC027121; AAH27121.2; -; mRNA.
DR EMBL; BC033605; AAH33605.2; -; mRNA.
DR CCDS; CCDS16088.1; -. [Q3UA16-2]
DR CCDS; CCDS57174.1; -. [Q3UA16-1]
DR RefSeq; NP_001186052.1; NM_001199123.2. [Q3UA16-1]
DR RefSeq; NP_001186053.1; NM_001199124.2. [Q3UA16-1]
DR RefSeq; NP_001292729.1; NM_001305800.1. [Q3UA16-1]
DR RefSeq; NP_079841.1; NM_025565.4. [Q3UA16-2]
DR RefSeq; XP_006500066.1; XM_006500003.3. [Q3UA16-1]
DR AlphaFoldDB; Q3UA16; -.
DR SMR; Q3UA16; -.
DR ComplexPortal; CPX-551; Ndc80 complex.
DR STRING; 10090.ENSMUSP00000107939; -.
DR iPTMnet; Q3UA16; -.
DR PhosphoSitePlus; Q3UA16; -.
DR EPD; Q3UA16; -.
DR MaxQB; Q3UA16; -.
DR PaxDb; Q3UA16; -.
DR PeptideAtlas; Q3UA16; -.
DR PRIDE; Q3UA16; -.
DR ProteomicsDB; 257552; -. [Q3UA16-1]
DR ProteomicsDB; 257553; -. [Q3UA16-2]
DR ProteomicsDB; 257554; -. [Q3UA16-3]
DR Antibodypedia; 33800; 214 antibodies from 22 providers.
DR DNASU; 66442; -.
DR Ensembl; ENSMUST00000005365; ENSMUSP00000005365; ENSMUSG00000005233. [Q3UA16-1]
DR Ensembl; ENSMUST00000112320; ENSMUSP00000107939; ENSMUSG00000005233. [Q3UA16-1]
DR Ensembl; ENSMUST00000167875; ENSMUSP00000128039; ENSMUSG00000005233. [Q3UA16-2]
DR GeneID; 66442; -.
DR KEGG; mmu:66442; -.
DR UCSC; uc008jxu.3; mouse. [Q3UA16-1]
DR UCSC; uc008jxx.3; mouse. [Q3UA16-3]
DR CTD; 57405; -.
DR MGI; MGI:1913692; Spc25.
DR VEuPathDB; HostDB:ENSMUSG00000005233; -.
DR eggNOG; KOG4657; Eukaryota.
DR GeneTree; ENSGT00390000002220; -.
DR HOGENOM; CLU_102420_0_0_1; -.
DR InParanoid; Q3UA16; -.
DR OMA; QGDYEVT; -.
DR OrthoDB; 1460234at2759; -.
DR PhylomeDB; Q3UA16; -.
DR TreeFam; TF332941; -.
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; 66442; 23 hits in 55 CRISPR screens.
DR ChiTaRS; Spc25; mouse.
DR PRO; PR:Q3UA16; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UA16; protein.
DR Bgee; ENSMUSG00000005233; Expressed in ear vesicle and 208 other tissues.
DR ExpressionAtlas; Q3UA16; baseline and differential.
DR Genevisible; Q3UA16; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0031262; C:Ndc80 complex; ISS:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR InterPro; IPR045143; Spc25.
DR InterPro; IPR013255; Spc25_C.
DR PANTHER; PTHR14281; PTHR14281; 1.
DR Pfam; PF08234; Spindle_Spc25; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..226
FT /note="Kinetochore protein Spc25"
FT /id="PRO_0000249566"
FT REGION 1..146
FT /note="Interaction with the N-terminus of SPBC24"
FT /evidence="ECO:0000250"
FT REGION 1..58
FT /note="Interaction with the NDC80-NUF2 subcomplex"
FT /evidence="ECO:0000250"
FT REGION 147..226
FT /note="Interaction with the C-terminus of SPBC24"
FT /evidence="ECO:0000250"
FT COILED 72..128
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBM1"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020518"
FT VAR_SEQ 154..162
FT /note="NKLQFIFTS -> KFLALLCRG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020519"
SQ SEQUENCE 226 AA; 26457 MW; A29FFD5B99F5D54A CRC64;
MGEDELALLN QSINEFGDKF RNRLDDNHSQ VLGLRDAFKD SMKAFSEKMS LKLKEEERMT
EMILEYKNQL CKQNKLIQEK KENVLKMIAE VKGKEQESEE LTAKIQELKE EYARKRETIS
TANKANEERL KGLQKSADLY RDYLGLEIRK IHGNKLQFIF TSIDPKNPES PYMFSMSINE
AKEYEVYDSS PHLECLAEFQ EKVRKTNNFS AFLANIRKAF IAKVHN
