NDC80_MOUSE
ID NDC80_MOUSE Reviewed; 642 AA.
AC Q9D0F1; Q3TQT6; Q3UWM5; Q99P70;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Kinetochore protein NDC80 homolog;
DE AltName: Full=Kinetochore protein Hec1;
DE AltName: Full=Kinetochore-associated protein 2;
GN Name=Ndc80; Synonyms=Hec1, Kntc2;
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 [MRNA].
RX PubMed=11266451; DOI=10.1083/jcb.152.2.349;
RA Wigge P.A., Kilmartin J.V.;
RT "The Ndc80p complex from Saccharomyces cerevisiae contains conserved
RT centromere components and has a function in chromosome segregation.";
RL J. Cell Biol. 152:349-360(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=9315664; DOI=10.1128/mcb.17.10.6049;
RA Chen Y., Riley D.J., Chen P.-L., Lee W.-H.;
RT "HEC, a novel nuclear protein rich in leucine heptad repeats specifically
RT involved in mitosis.";
RL Mol. Cell. Biol. 17:6049-6056(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP 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. Plays a role in
CC chromosome congression and is essential for the end-on attachment of
CC the kinetochores to spindle microtubules.
CC {ECO:0000250|UniProtKB:O14777}.
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. Interacts with NEK2 and ZWINT specifically during mitosis.
CC Interacts with CENPH and MIS12. May interact with AURKB, PSMC2, PSMC5
CC and SMC1A. May interact with RB1 during G2 phase and mitosis. Interacts
CC with CKAP5 (By similarity). Interacts with CDT1; leading to kinetochore
CC localization of CDT1 (By similarity). {ECO:0000250|UniProtKB:O14777}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14777}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O14777}.
CC Note=Localizes to kinetochores from late prophase to anaphase.
CC Localizes specifically to the outer plate of the kinetochore.
CC {ECO:0000250|UniProtKB:O14777}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, testis and thymus.
CC {ECO:0000269|PubMed:9315664}.
CC -!- PTM: Phosphorylation begins in S phase of the cell cycle and peaks in
CC mitosis. Phosphorylated by NEK2. Also phosphorylated by AURKA and
CC AURKB. {ECO:0000250|UniProtKB:O14777}.
CC -!- PTM: Acetylated at Lys-53 and Lys-59 by KAT5 during mitosis, promoting
CC robust kinetochore-microtubule attachment. Deacetylated by SIRT1.
CC {ECO:0000250|UniProtKB:O14777}.
CC -!- SIMILARITY: Belongs to the NDC80/HEC1 family. {ECO:0000305}.
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DR EMBL; AF326730; AAK01425.1; -; mRNA.
DR EMBL; AK011497; BAB27657.1; -; mRNA.
DR EMBL; AK136236; BAE22889.1; -; mRNA.
DR EMBL; AK163317; BAE37296.1; -; mRNA.
DR EMBL; AK169427; BAE41169.1; -; mRNA.
DR EMBL; BC020131; AAH20131.1; -; mRNA.
DR CCDS; CCDS28959.1; -.
DR RefSeq; NP_075783.2; NM_023294.2.
DR AlphaFoldDB; Q9D0F1; -.
DR SMR; Q9D0F1; -.
DR BioGRID; 211904; 57.
DR ComplexPortal; CPX-551; Ndc80 complex.
DR IntAct; Q9D0F1; 54.
DR MINT; Q9D0F1; -.
DR STRING; 10090.ENSMUSP00000024851; -.
DR iPTMnet; Q9D0F1; -.
DR PhosphoSitePlus; Q9D0F1; -.
DR EPD; Q9D0F1; -.
DR jPOST; Q9D0F1; -.
DR MaxQB; Q9D0F1; -.
DR PaxDb; Q9D0F1; -.
DR PeptideAtlas; Q9D0F1; -.
DR PRIDE; Q9D0F1; -.
DR ProteomicsDB; 293637; -.
DR Antibodypedia; 6039; 463 antibodies from 39 providers.
DR DNASU; 67052; -.
DR Ensembl; ENSMUST00000024851; ENSMUSP00000024851; ENSMUSG00000024056.
DR GeneID; 67052; -.
DR KEGG; mmu:67052; -.
DR UCSC; uc008dmk.2; mouse.
DR CTD; 10403; -.
DR MGI; MGI:1914302; Ndc80.
DR VEuPathDB; HostDB:ENSMUSG00000024056; -.
DR eggNOG; KOG0995; Eukaryota.
DR GeneTree; ENSGT00390000018386; -.
DR HOGENOM; CLU_012583_2_0_1; -.
DR InParanoid; Q9D0F1; -.
DR OMA; IRFKVHV; -.
DR OrthoDB; 925552at2759; -.
DR PhylomeDB; Q9D0F1; -.
DR TreeFam; TF101177; -.
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; 67052; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Ndc80; mouse.
DR PRO; PR:Q9D0F1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D0F1; protein.
DR Bgee; ENSMUSG00000024056; Expressed in humerus cartilage element and 132 other tissues.
DR ExpressionAtlas; Q9D0F1; baseline and differential.
DR Genevisible; Q9D0F1; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0031262; C:Ndc80 complex; ISS:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000940; C:outer kinetochore; ISO:MGI.
DR GO; GO:0030332; F:cyclin binding; IPI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0140483; F:kinetochore adaptor activity; ISS:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
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:0051298; P:centrosome duplication; ISO:MGI.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0008315; P:G2/MI transition of meiotic cell cycle; IDA:MGI.
DR GO; GO:0051383; P:kinetochore organization; IMP:MGI.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISO:MGI.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP:MGI.
DR Gene3D; 1.10.418.30; -; 1.
DR InterPro; IPR040967; DUF5595.
DR InterPro; IPR005550; Kinetochore_Ndc80.
DR InterPro; IPR038273; Ndc80_sf.
DR PANTHER; PTHR10643; PTHR10643; 1.
DR Pfam; PF18077; DUF5595; 1.
DR Pfam; PF03801; Ndc80_HEC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..642
FT /note="Kinetochore protein NDC80 homolog"
FT /id="PRO_0000249552"
FT REGION 1..445
FT /note="Interaction with the N-terminus of CDCA1"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 1..250
FT /note="Nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 128..251
FT /note="Interaction with RB1"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 251..618
FT /note="Interaction with NEK2 and ZWINT"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 251..431
FT /note="Interaction with SMC1A"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 361..547
FT /note="Interaction with PSMC2 and SMC1A"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT REGION 446..642
FT /note="Interaction with the C-terminus of CDCA1 and the
FT SPBC24-SPBC25 subcomplex"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT COILED 240..403
FT /evidence="ECO:0000255"
FT COILED 458..639
FT /evidence="ECO:0000255"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 165
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14777"
FT CONFLICT 13
FT /note="R -> S (in Ref. 2; BAE37296)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> E (in Ref. 1; AAK01425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 73962 MW; 2BFF61F09B6E2CF8 CRC64;
MKRSSVSTCG AGRLSMQELR TLDLNKPGLY TPQTKERSTF GKLSTHKPTS ERKVSIFGKR
TSGHGSRNSQ LGIFSSSEKI KDPRPLNDKA FIQQCIRQLY EFLTENGYVY SVSMKSLQAP
STKEFLKIFA FLYGFLCPSY ELPGTKCEEE VPRIFKALGY PFTLSKSSMY TVGAPHTWPH
IVAALVWLID CIKIDTAMKE SSPLFDDGQL WGEETEDGIK HNKLFLEYTK KCYEKFMTGA
DSFEEEDAEL QAKLKDLYKV DASKLESLEA ENKALNEQIA RLEEEREREP NRLMSLKKLK
ASLQADVQNY KAYMSNLESH LAVLKQKSNS LDEEIGRVEQ ECETVKQENT RLQSIVDNQK
YSVADIERIN HEKNELQQTI NKLTKDLEAE QQQMWNEELK YARGKEAIEA QLAEYHKLAR
KLKLIPKGAE NSKGYDFEIK FNPEAGANCL VKYRTQVYAP LKELLNESEE EINKALNKKR
HLEDTLEQLN TMKTESKNTV RMLKEEIQKL DDLHQQAVKE AEEKDKKSAS ELESLEKHKH
LLESGVNDGL SEAMDELDAV QREYQLTVKT TTEERRKVEN NLQRLLEMVA THVGSLEKHL
EEENAKADRE YEEFMSEDLL ENIREMAEKY KRNAAQLKAP DK
