NUF2_YEAST
ID NUF2_YEAST Reviewed; 451 AA.
AC P33895; D6W1Z8; Q6B1X5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Kinetochore protein NUF2;
GN Name=NUF2; OrderedLocusNames=YOL069W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-338; ILE-340;
RP TYR-383; LEU-410; LYS-441 AND MET-446.
RC STRAIN=W303A;
RX PubMed=8188751; DOI=10.1083/jcb.125.4.853;
RA Osborne M.A., Schlenstedt G., Jinks T., Silver P.A.;
RT "Nuf2, a spindle pole body-associated protein required for nuclear division
RT in yeast.";
RL J. Cell Biol. 125:853-866(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPC24 AND SPC25.
RX PubMed=11179222; DOI=10.1093/emboj/20.4.777;
RA Janke C., Ortiz J., Lechner J., Shevchenko A., Shevchenko A., Magiera M.M.,
RA Schramm C., Schiebel E.;
RT "The budding yeast proteins Spc24p and Spc25p interact with Ndc80p and
RT Nuf2p at the kinetochore and are important for kinetochore clustering and
RT checkpoint control.";
RL EMBO J. 20:777-791(2001).
RN [7]
RP FUNCTION OF THE NDC80 COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION IN
RP THE NDC80 COMPLEX.
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 [8]
RP FUNCTION OF THE NDC80 COMPLEX.
RX PubMed=12514103; DOI=10.1101/gad.1040903;
RA McCleland M.L., Gardner R.D., Kallio M.J., Daum J.R., Gorbsky G.J.,
RA Burke D.J., Stukenberg P.T.;
RT "The highly conserved Ndc80 complex is required for kinetochore assembly,
RT chromosome congression, and spindle checkpoint activity.";
RL Genes Dev. 17:101-114(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP IDENTIFICATION IN THE NDC80 COMPLEX.
RX PubMed=15371542; DOI=10.1091/mbc.e04-06-0443;
RA Kerres A., Vietmeier-Decker C., Ortiz J., Karig I., Beuter C., Hegemann J.,
RA Lechner J., Fleig U.;
RT "The fission yeast kinetochore component Spc7 associates with the EB1
RT family member Mal3 and is required for kinetochore-spindle association.";
RL Mol. Biol. Cell 15:5255-5267(2004).
RN [11]
RP 3D-STRUCTURE MODELING OF THE NDC80 COMPLEX.
RX PubMed=15809444; DOI=10.1073/pnas.0501168102;
RA Wei R.R., Sorger P.K., Harrison S.C.;
RT "Molecular organization of the Ndc80 complex, an essential kinetochore
RT component.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5363-5367(2005).
CC -!- FUNCTION: Acts as component of the essential kinetochore-associated
CC NDC80 complex, which is involved in chromosome segregation and spindle
CC checkpoint activity. {ECO:0000269|PubMed:11266451,
CC ECO:0000269|PubMed:12514103}.
CC -!- SUBUNIT: Component of the NDC80 complex, which consists of TID3/NDC80,
CC NUF2, SPC24 and SPC25. The NDC80 complex is formed by two subcomplexes,
CC TID3/NDC80-NUF2 and SPC24-SPC25, which are joined end-to-end through
CC their coiled-coil domains. It has a rod-like structure with a length of
CC 570 Angstroms and globular domains at either end. The TID3/NDC80-NUF2
CC globular domains are probably directed to microtubules, the SPC24-SPC25
CC globular domains to the centromere. {ECO:0000269|PubMed:11266451,
CC ECO:0000269|PubMed:15371542}.
CC -!- INTERACTION:
CC P33895; P43618: CNN1; NbExp=2; IntAct=EBI-12377, EBI-23036;
CC P33895; P40460: NDC80; NbExp=15; IntAct=EBI-12377, EBI-25247;
CC P33895; Q04477: SPC24; NbExp=8; IntAct=EBI-12377, EBI-27228;
CC P33895; P40014: SPC25; NbExp=6; IntAct=EBI-12377, EBI-22458;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Associated with kinetochores.
CC -!- MISCELLANEOUS: Present with 1550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NUF2 family. {ECO:0000305}.
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DR EMBL; X72225; CAA51028.1; -; Genomic_DNA.
DR EMBL; Z74811; CAA99079.1; -; Genomic_DNA.
DR EMBL; AY692955; AAT92974.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10714.1; -; Genomic_DNA.
DR PIR; A53910; A53910.
DR RefSeq; NP_014572.1; NM_001183324.1.
DR PDB; 5TCS; X-ray; 2.83 A; B=2-153, B=407-451.
DR PDB; 5TD8; X-ray; 7.53 A; B=1-153, B=407-451.
DR PDB; 7KDF; X-ray; 2.72 A; B=2-172.
DR PDBsum; 5TCS; -.
DR PDBsum; 5TD8; -.
DR PDBsum; 7KDF; -.
DR AlphaFoldDB; P33895; -.
DR SMR; P33895; -.
DR BioGRID; 34332; 353.
DR ComplexPortal; CPX-548; NDC80 complex.
DR DIP; DIP-1481N; -.
DR IntAct; P33895; 31.
DR MINT; P33895; -.
DR STRING; 4932.YOL069W; -.
DR MaxQB; P33895; -.
DR PaxDb; P33895; -.
DR PRIDE; P33895; -.
DR EnsemblFungi; YOL069W_mRNA; YOL069W; YOL069W.
DR GeneID; 854085; -.
DR KEGG; sce:YOL069W; -.
DR SGD; S000005430; NUF2.
DR VEuPathDB; FungiDB:YOL069W; -.
DR eggNOG; KOG4438; Eukaryota.
DR GeneTree; ENSGT00390000004199; -.
DR HOGENOM; CLU_025461_2_0_1; -.
DR InParanoid; P33895; -.
DR OMA; AHIKLYI; -.
DR BioCyc; YEAST:G3O-33474-MON; -.
DR PRO; PR:P33895; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P33895; protein.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0031262; C:Ndc80 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IGI:SGD.
DR GO; GO:0051383; P:kinetochore organization; IBA:GO_Central.
DR GO; GO:0045132; P:meiotic chromosome segregation; IBA:GO_Central.
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 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..451
FT /note="Kinetochore protein NUF2"
FT /id="PRO_0000057995"
FT COILED 153..291
FT /evidence="ECO:0000255"
FT COILED 341..371
FT /evidence="ECO:0000255"
FT COILED 398..432
FT /evidence="ECO:0000255"
FT MUTAGEN 338
FT /note="T->P: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8188751"
FT MUTAGEN 340
FT /note="I->K: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8188751"
FT MUTAGEN 383
FT /note="Y->C: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8188751"
FT MUTAGEN 410
FT /note="L->S: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8188751"
FT MUTAGEN 441
FT /note="K->I: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8188751"
FT MUTAGEN 446
FT /note="M->L: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:8188751"
FT CONFLICT 240
FT /note="N -> Y (in Ref. 5; AAT92974)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:7KDF"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5TCS"
FT HELIX 79..99
FT /evidence="ECO:0007829|PDB:7KDF"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 116..136
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:7KDF"
SQ SEQUENCE 451 AA; 52973 MW; D58796E1B5D1E772 CRC64;
MSRNQDVFPI LDLQELVICL QSCDFALATQ ENISRPTSDY MVTLYKQIIE NFMGISVESL
LNSSNQETGD GHLQEENENI YLDTLNVLVL NKICFKFFEN IGVQDFNMTD LYKPEAQRTQ
RLLSAVVNYA RFREERMFDC NSFILQMESL LGQLRSKFDD YNLIQQQLKQ YEDVDGDNIP
DEQELQKLEE QNKELEIQLK KLTKIQETLS IDYNDYKISK QSIFKDLEAL SFQIVELESN
RDKLIKISNT DMEELSEGIK ELNDLLIQRK KTLDDLTAQQ KNLQDTVTTF ETIISELYDV
LRIISSEVQE SNRTETELVG LKQNLINNKL KLMNVLETGI MYKLEILQEQ LDLQLKNLEK
LSQDTKEESR LNDTKLMDLQ IKYENEIKPK IDKTDIFIQE ELISGKINKL NDEIKQLQKD
FEVEVKEIEI EYSLLSGHIN KYMNEMLEYM Q
