NUF2_MOUSE
ID NUF2_MOUSE Reviewed; 463 AA.
AC Q99P69; Q8BTK7; Q8VE05; Q9CST5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Kinetochore protein Nuf2;
DE AltName: Full=Cell division cycle-associated protein 1;
GN Name=Nuf2; Synonyms=Cdca1, Nuf2r;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Colon, Egg, and Skin;
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] (ISOFORM 1).
RC STRAIN=Czech II; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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:Q9BZD4}.
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. May interact with AURKB/Aurora-B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Note=Localizes to kinetochores from late
CC prophase to anaphase. Localizes specifically to the outer plate of the
CC kinetochore (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99P69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99P69-2; Sequence=VSP_020553, VSP_020554;
CC -!- PTM: Can be phosphorylated by AURKA and AURKB. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NUF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41008.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF326732; AAK01427.1; -; mRNA.
DR EMBL; AK012011; BAB27973.1; -; mRNA.
DR EMBL; AK089939; BAC41008.1; ALT_FRAME; mRNA.
DR EMBL; AK132467; BAE21183.1; -; mRNA.
DR EMBL; AK162249; BAE36815.1; -; mRNA.
DR EMBL; BC020026; AAH20026.1; -; mRNA.
DR CCDS; CCDS15463.1; -. [Q99P69-1]
DR RefSeq; NP_075773.2; NM_023284.3. [Q99P69-1]
DR RefSeq; XP_006497021.1; XM_006496958.1.
DR AlphaFoldDB; Q99P69; -.
DR SMR; Q99P69; -.
DR ComplexPortal; CPX-551; Ndc80 complex.
DR STRING; 10090.ENSMUSP00000106999; -.
DR iPTMnet; Q99P69; -.
DR PhosphoSitePlus; Q99P69; -.
DR EPD; Q99P69; -.
DR MaxQB; Q99P69; -.
DR PaxDb; Q99P69; -.
DR PeptideAtlas; Q99P69; -.
DR PRIDE; Q99P69; -.
DR ProteomicsDB; 295462; -. [Q99P69-1]
DR ProteomicsDB; 295463; -. [Q99P69-2]
DR Antibodypedia; 34328; 203 antibodies from 29 providers.
DR Ensembl; ENSMUST00000028000; ENSMUSP00000028000; ENSMUSG00000026683. [Q99P69-1]
DR Ensembl; ENSMUST00000111368; ENSMUSP00000106999; ENSMUSG00000026683. [Q99P69-1]
DR GeneID; 66977; -.
DR KEGG; mmu:66977; -.
DR UCSC; uc007dlj.1; mouse. [Q99P69-1]
DR UCSC; uc007dll.1; mouse. [Q99P69-2]
DR CTD; 83540; -.
DR MGI; MGI:1914227; Nuf2.
DR VEuPathDB; HostDB:ENSMUSG00000026683; -.
DR eggNOG; KOG4438; Eukaryota.
DR GeneTree; ENSGT00390000004199; -.
DR HOGENOM; CLU_589957_0_0_1; -.
DR InParanoid; Q99P69; -.
DR OMA; AHIKLYI; -.
DR OrthoDB; 752521at2759; -.
DR PhylomeDB; Q99P69; -.
DR TreeFam; TF101067; -.
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; 66977; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Nuf2; mouse.
DR PRO; PR:Q99P69; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q99P69; protein.
DR Bgee; ENSMUSG00000026683; Expressed in spermatocyte and 203 other tissues.
DR ExpressionAtlas; Q99P69; baseline and differential.
DR Genevisible; Q99P69; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
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; IC:ComplexPortal.
DR GO; GO:0051383; P:kinetochore organization; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR Gene3D; 1.10.418.60; -; 1.
DR InterPro; IPR005549; Kinetochore_Nuf2_N.
DR InterPro; IPR038275; Nuf2_N_sf.
DR Pfam; PF03800; Nuf2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..463
FT /note="Kinetochore protein Nuf2"
FT /id="PRO_0000249814"
FT REGION 1..385
FT /note="Interaction with the N-terminus of NDC80"
FT /evidence="ECO:0000250"
FT REGION 386..463
FT /note="Interaction with the C-terminus of NDC80 and the
FT SPBC24-SPBC25 subcomplex"
FT /evidence="ECO:0000250"
FT COILED 149..341
FT /evidence="ECO:0000255"
FT COILED 389..463
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZD4"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 270..296
FT /note="EKVMEQYDIYRDSVDCLPSCQLEVQLY -> VSRFTLWHSLNYLVSVQISLL
FT NFYAPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020553"
FT VAR_SEQ 297..429
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020554"
FT CONFLICT 4
FT /note="L -> W (in Ref. 2; BAC41008)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="L -> R (in Ref. 2; BAC41008)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="V -> G (in Ref. 2; BAB27973)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="K -> E (in Ref. 1; AAK01427)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="Q -> P (in Ref. 2; BAC41008)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="N -> H (in Ref. 2; BAC41008)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="K -> Q (in Ref. 2; BAC41008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 54594 MW; 7330FFDB6E28AEAC CRC64;
METLSFPRYN VAELVVHIRN KLLTGADGKN LSKSDFLPNP KSDVLYMIYM KALQLVYGVR
LEHFYMMPMN IEVTYPHLME GFLPVRSLFF YMDSFMPICR VNDFEIVDIL NPRTNRTSRF
LSGIINFIHF RETCLEKCEE FLLQNKSSMV RMQQLSNVHQ EALMKLEKLN TVPAEEREEF
KQFMDDIQEL QHLLNEEFRQ KTTLLQEEYA KMKSDISEKT KHLNEQKLSL VSLKEVEDNL
KSKIVDSPEK LKNYKDKMKG TVQKLRSARE KVMEQYDIYR DSVDCLPSCQ LEVQLYQKKS
QDLADNREKL SSLLKESLNL EDQIESDSSE LKKLKTEENS LIRMTTVKKE KLATARFKIN
KKQEDVKHYK QAMIEDCNKV QEKRDAVCEQ VTTVNQEIHK IKSAIQQLRD TKKREILKSQ
EIFVNLKSAL EKYHEGIEKV AEERSAKLEE KTAELKKRMV RMV
