NUF2_HUMAN
ID NUF2_HUMAN Reviewed; 464 AA.
AC Q9BZD4; Q8WU69; Q96HJ4; Q96Q78;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Kinetochore protein Nuf2;
DE Short=hNuf2;
DE Short=hNuf2R;
DE Short=hsNuf2;
DE AltName: Full=Cell division cycle-associated protein 1;
GN Name=NUF2; Synonyms=CDCA1, NUF2R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-229.
RX PubMed=11685532; DOI=10.1007/s004120100153;
RA Nabetani A., Koujin T., Tsutsumi C., Haraguchi T., Hiraoka Y.;
RT "A conserved protein, Nuf2, is implicated in connecting the centromere to
RT the spindle during chromosome segregation: a link between the kinetochore
RT function and the spindle checkpoint.";
RL Chromosoma 110:322-334(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-229.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Chronic myeloid leukemia cell, and Lung;
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 [6]
RP FUNCTION.
RX PubMed=12438418; DOI=10.1083/jcb.200208159;
RA DeLuca J.G., Moree B., Hickey J.M., Kilmartin J.V., Salmon E.D.;
RT "hNuf2 inhibition blocks stable kinetochore-microtubule attachment and
RT induces mitotic cell death in HeLa cells.";
RL J. Cell Biol. 159:549-555(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14654001; DOI=10.1016/j.cub.2003.10.056;
RA DeLuca J.G., Howell B.J., Canman J.C., Hickey J.M., Fang G., Salmon E.D.;
RT "Nuf2 and Hec1 are required for retention of the checkpoint proteins Mad1
RT and Mad2 to kinetochores.";
RL Curr. Biol. 13:2103-2109(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15235793; DOI=10.1007/s00412-004-0288-2;
RA Stucke V.M., Baumann C., Nigg E.A.;
RT "Kinetochore localization and microtubule interaction of the human spindle
RT checkpoint kinase Mps1.";
RL Chromosoma 113:1-15(2004).
RN [9]
RP FUNCTION.
RX PubMed=15062103; DOI=10.1016/j.cub.2004.03.031;
RA Joseph J., Liu S.-T., Jablonski S.A., Yen T.J., Dasso M.;
RT "The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore
RT interactions in vivo.";
RL Curr. Biol. 14:611-617(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15239953; DOI=10.1016/j.devcel.2004.06.006;
RA Meraldi P., Draviam V.M., Sorger P.K.;
RT "Timing and checkpoints in the regulation of mitotic progression.";
RL Dev. Cell 7:45-60(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NDC80
RP COMPLEX.
RX PubMed=14699129; DOI=10.1074/jbc.m310224200;
RA Bharadwaj R., Qi W., Yu H.;
RT "Identification of two novel components of the human NDC80 kinetochore
RT complex.";
RL J. Biol. Chem. 279:13076-13085(2004).
RN [12]
RP INTERACTION WITH AURKB AND NDC80, AND PHOSPHORYLATION BY AURKA AND AURKB.
RX PubMed=14602875; DOI=10.1074/mcp.m300072-mcp200;
RA Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G.,
RA Lin W.-J., Still I.H., Huang C.-Y.F.;
RT "Identification of the substrates and interaction proteins of aurora
RT kinases from a protein-protein interaction model.";
RL Mol. Cell. Proteomics 3:93-104(2004).
RN [13]
RP CHARACTERIZATION OF THE NDC80 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15961401; DOI=10.1074/jbc.m504070200;
RA Ciferri C., De Luca J., Monzani S., Ferrari K.J., Ristic D., Wyman C.,
RA Stark H., Kilmartin J., Salmon E.D., Musacchio A.;
RT "Architecture of the human Ndc80-Hec1 complex, a critical constituent of
RT the outer kinetochore.";
RL J. Biol. Chem. 280:29088-29095(2005).
RN [14]
RP FUNCTION.
RX PubMed=15548592; DOI=10.1091/mbc.e04-09-0852;
RA DeLuca J.G., Dong Y., Hergert P., Strauss J., Hickey J.M., Salmon E.D.,
RA McEwen B.F.;
RT "Hec1 and Nuf2 are core components of the kinetochore outer plate essential
RT for organizing microtubule attachment sites.";
RL Mol. Biol. Cell 16:519-531(2005).
RN [15]
RP FUNCTION, INTERACTION WITH CENPE, AND SUBCELLULAR LOCATION.
RX PubMed=17535814; DOI=10.1074/jbc.m609026200;
RA Liu D., Ding X., Du J., Cai X., Huang Y., Ward T., Shaw A., Yang Y., Hu R.,
RA Jin C., Yao X.;
RT "Human NUF2 interacts with centromere-associated protein E and is essential
RT for a stable spindle microtubule-kinetochore attachment.";
RL J. Biol. Chem. 282:21415-21424(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION.
RX PubMed=23085020; DOI=10.1016/j.devcel.2012.09.012;
RA Schmidt J.C., Arthanari H., Boeszoermenyi A., Dashkevich N.M.,
RA Wilson-Kubalek E.M., Monnier N., Markus M., Oberer M., Milligan R.A.,
RA Bathe M., Wagner G., Grishchuk E.L., Cheeseman I.M.;
RT "The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and
RT binds to curved protofilaments.";
RL Dev. Cell 23:968-980(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 (PubMed:12438418, PubMed:14654001, PubMed:15062103,
CC PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:17535814).
CC Required for kinetochore integrity and the organization of stable
CC microtubule binding sites in the outer plate of the kinetochore
CC (PubMed:15548592). 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 (PubMed:23085020).
CC {ECO:0000269|PubMed:12438418, ECO:0000269|PubMed:14654001,
CC ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793,
CC ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592,
CC ECO:0000269|PubMed:17535814, ECO:0000269|PubMed:23085020}.
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. Directly interacts with
CC CENPE; this interaction determines CENPE kinetochore localization.
CC {ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14699129,
CC ECO:0000269|PubMed:17535814}.
CC -!- INTERACTION:
CC Q9BZD4; Q02224: CENPE; NbExp=9; IntAct=EBI-724102, EBI-1375040;
CC Q9BZD4; O14777: NDC80; NbExp=14; IntAct=EBI-724102, EBI-715849;
CC Q9BZD4; P33981-1: TTK; NbExp=2; IntAct=EBI-724102, EBI-15986834;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Localizes to kinetochores from late prophase to anaphase.
CC Localizes specifically to the outer plate of the kinetochore. NDC80 is
CC required for efficient kinetochore localization.
CC -!- PTM: Can be phosphorylated by AURKA and AURKB.
CC {ECO:0000269|PubMed:14602875}.
CC -!- SIMILARITY: Belongs to the NUF2 family. {ECO:0000305}.
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DR EMBL; AB050577; BAB59141.1; -; mRNA.
DR EMBL; AB050578; BAB59142.1; -; mRNA.
DR EMBL; AF326731; AAK01426.1; -; mRNA.
DR EMBL; AK093348; BAC04140.1; -; mRNA.
DR EMBL; AL592435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008489; AAH08489.1; -; mRNA.
DR EMBL; BC021171; AAH21171.2; -; mRNA.
DR CCDS; CCDS1245.1; -.
DR RefSeq; NP_113611.2; NM_031423.3.
DR RefSeq; NP_663735.2; NM_145697.2.
DR PDB; 2VE7; X-ray; 2.88 A; C/D=1-169.
DR PDB; 3IZ0; EM; -; D/F=1-169.
DR PDBsum; 2VE7; -.
DR PDBsum; 3IZ0; -.
DR AlphaFoldDB; Q9BZD4; -.
DR SMR; Q9BZD4; -.
DR BioGRID; 123673; 113.
DR ComplexPortal; CPX-550; Ndc80 complex.
DR CORUM; Q9BZD4; -.
DR DIP; DIP-36119N; -.
DR IntAct; Q9BZD4; 49.
DR MINT; Q9BZD4; -.
DR STRING; 9606.ENSP00000271452; -.
DR iPTMnet; Q9BZD4; -.
DR PhosphoSitePlus; Q9BZD4; -.
DR BioMuta; NUF2; -.
DR DMDM; 115311829; -.
DR EPD; Q9BZD4; -.
DR jPOST; Q9BZD4; -.
DR MassIVE; Q9BZD4; -.
DR MaxQB; Q9BZD4; -.
DR PaxDb; Q9BZD4; -.
DR PeptideAtlas; Q9BZD4; -.
DR PRIDE; Q9BZD4; -.
DR ProteomicsDB; 79815; -.
DR Antibodypedia; 34328; 203 antibodies from 29 providers.
DR DNASU; 83540; -.
DR Ensembl; ENST00000271452.8; ENSP00000271452.3; ENSG00000143228.13.
DR Ensembl; ENST00000367900.7; ENSP00000356875.3; ENSG00000143228.13.
DR GeneID; 83540; -.
DR KEGG; hsa:83540; -.
DR MANE-Select; ENST00000271452.8; ENSP00000271452.3; NM_145697.3; NP_663735.2.
DR UCSC; uc001gcq.2; human.
DR CTD; 83540; -.
DR DisGeNET; 83540; -.
DR GeneCards; NUF2; -.
DR HGNC; HGNC:14621; NUF2.
DR HPA; ENSG00000143228; Group enriched (bone marrow, lymphoid tissue, testis).
DR MalaCards; NUF2; -.
DR MIM; 611772; gene.
DR neXtProt; NX_Q9BZD4; -.
DR OpenTargets; ENSG00000143228; -.
DR PharmGKB; PA162398215; -.
DR VEuPathDB; HostDB:ENSG00000143228; -.
DR eggNOG; KOG4438; Eukaryota.
DR GeneTree; ENSGT00390000004199; -.
DR InParanoid; Q9BZD4; -.
DR OMA; AHIKLYI; -.
DR OrthoDB; 752521at2759; -.
DR PhylomeDB; Q9BZD4; -.
DR TreeFam; TF101067; -.
DR PathwayCommons; Q9BZD4; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q9BZD4; -.
DR SIGNOR; Q9BZD4; -.
DR BioGRID-ORCS; 83540; 767 hits in 1056 CRISPR screens.
DR EvolutionaryTrace; Q9BZD4; -.
DR GeneWiki; NUF2; -.
DR GenomeRNAi; 83540; -.
DR Pharos; Q9BZD4; Tbio.
DR PRO; PR:Q9BZD4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZD4; protein.
DR Bgee; ENSG00000143228; Expressed in ventricular zone and 123 other tissues.
DR ExpressionAtlas; Q9BZD4; baseline and differential.
DR Genevisible; Q9BZD4; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031262; C:Ndc80 complex; IDA:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; NAS:UniProtKB.
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 IDEAL; IID00393; -.
DR InterPro; IPR005549; Kinetochore_Nuf2_N.
DR InterPro; IPR038275; Nuf2_N_sf.
DR Pfam; PF03800; Nuf2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..464
FT /note="Kinetochore protein Nuf2"
FT /id="PRO_0000249813"
FT REGION 1..385
FT /note="Interaction with the N-terminus of NDC80"
FT REGION 386..464
FT /note="Interaction with the C-terminus of NDC80 and the
FT SPBC24-SPBC25 subcomplex"
FT COILED 147..345
FT /evidence="ECO:0000255"
FT COILED 389..459
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 229
FT /note="S -> L (in dbSNP:rs11802875)"
FT /evidence="ECO:0000269|PubMed:11266451,
FT ECO:0000269|PubMed:11685532"
FT /id="VAR_027490"
FT VARIANT 239
FT /note="S -> R (in dbSNP:rs16852767)"
FT /id="VAR_027491"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2VE7"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:2VE7"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 114..144
FT /evidence="ECO:0007829|PDB:2VE7"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:2VE7"
SQ SEQUENCE 464 AA; 54304 MW; 250BFED5AD87153B CRC64;
METLSFPRYN VAEIVIHIRN KILTGADGKN LTKNDLYPNP KPEVLHMIYM RALQIVYGIR
LEHFYMMPVN SEVMYPHLME GFLPFSNLVT HLDSFLPICR VNDFETADIL CPKAKRTSRF
LSGIINFIHF REACRETYME FLWQYKSSAD KMQQLNAAHQ EALMKLERLD SVPVEEQEEF
KQLSDGIQEL QQSLNQDFHQ KTIVLQEGNS QKKSNISEKT KRLNELKLSV VSLKEIQESL
KTKIVDSPEK LKNYKEKMKD TVQKLKNARQ EVVEKYEIYG DSVDCLPSCQ LEVQLYQKKI
QDLSDNREKL ASILKESLNL EDQIESDESE LKKLKTEENS FKRLMIVKKE KLATAQFKIN
KKHEDVKQYK RTVIEDCNKV QEKRGAVYER VTTINQEIQK IKLGIQQLKD AAEREKLKSQ
EIFLNLKTAL EKYHDGIEKA AEDSYAKIDE KTAELKRKMF KMST
