NKP2_YEAST
ID NKP2_YEAST Reviewed; 153 AA.
AC Q06162; D6VYV9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Inner kinetochore subunit NKP2 {ECO:0000305};
DE AltName: Full=Constitutive centromere-associated network protein NKP2 {ECO:0000305};
DE AltName: Full=Non-essential kinetochore protein 2;
GN Name=NKP2; OrderedLocusNames=YLR315W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF CTF19 COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12408861; DOI=10.1016/s0092-8674(02)00973-x;
RA Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,
RA Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
RT "Phospho-regulation of kinetochore-microtubule attachments by the Aurora
RT kinase Ipl1p.";
RL Cell 111:163-172(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP IDENTIFICATION IN CCAN, AND SUBUNIT.
RX PubMed=22561346; DOI=10.1038/ncb2493;
RA Schleiffer A., Maier M., Litos G., Lampert F., Hornung P., Mechtler K.,
RA Westermann S.;
RT "CENP-T proteins are conserved centromere receptors of the Ndc80 complex.";
RL Nat. Cell Biol. 14:604-613(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=29046335; DOI=10.15252/embj.201796636;
RA Schmitzberger F., Richter M.M., Gordiyenko Y., Robinson C.V., Dadlez M.,
RA Westermann S.;
RT "Molecular basis for inner kinetochore configuration through RWD domain-
RT peptide interactions.";
RL EMBO J. 36:3458-3482(2017).
CC -!- FUNCTION: Component of the kinetochore, a multiprotein complex that
CC assembles on centromeric DNA and attaches chromosomes to spindle
CC microtubules, mediating chromosome segregation and sister chromatid
CC segregation during meiosis and mitosis. Component of the inner
CC kinetochore constitutive centromere-associated network (CCAN), which
CC serves as a structural platform for outer kinetochore assembly.
CC {ECO:0000269|PubMed:22561346}.
CC -!- SUBUNIT: Component of the inner kinetochore constitutive centromere-
CC associated network (CCAN) (also known as central kinetochore CTF19
CC complex in yeast), which is composed of at least AME1, CHL4, CNN1,
CC CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2,
CC OKP1 and WIP1 (PubMed:22561346). NKP1 interacts directly with OKP1 and
CC AME1 (By similarity). {ECO:0000250|UniProtKB:Q6CSR8,
CC ECO:0000269|PubMed:22561346}.
CC -!- INTERACTION:
CC Q06162; Q12493: NKP1; NbExp=3; IntAct=EBI-34256, EBI-35840;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12408861,
CC ECO:0000269|PubMed:29046335}. Note=Associated with kinetochores
CC (PubMed:12408861).
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NKP2 family. {ECO:0000305}.
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DR EMBL; U20618; AAB64519.1; -; Genomic_DNA.
DR EMBL; AY692848; AAT92867.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09625.1; -; Genomic_DNA.
DR PIR; S53394; S53394.
DR RefSeq; NP_013419.1; NM_001182204.1.
DR PDB; 6NUW; EM; 4.25 A; J=1-153.
DR PDB; 6QLD; EM; 4.15 A; Z=3-153.
DR PDB; 6QLE; EM; 3.55 A; Z=1-153.
DR PDB; 6QLF; EM; 3.45 A; Z=1-153.
DR PDBsum; 6NUW; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6QLF; -.
DR AlphaFoldDB; Q06162; -.
DR SMR; Q06162; -.
DR BioGRID; 31580; 261.
DR ComplexPortal; CPX-1156; Central kinetochore CTF19 complex.
DR DIP; DIP-1939N; -.
DR IntAct; Q06162; 8.
DR MINT; Q06162; -.
DR STRING; 4932.YLR315W; -.
DR PaxDb; Q06162; -.
DR PRIDE; Q06162; -.
DR EnsemblFungi; YLR315W_mRNA; YLR315W; YLR315W.
DR GeneID; 851025; -.
DR KEGG; sce:YLR315W; -.
DR SGD; S000004307; NKP2.
DR VEuPathDB; FungiDB:YLR315W; -.
DR eggNOG; ENOG502SFRX; Eukaryota.
DR HOGENOM; CLU_135200_0_0_1; -.
DR InParanoid; Q06162; -.
DR OMA; ATCTETR; -.
DR BioCyc; YEAST:G3O-32401-MON; -.
DR PRO; PR:Q06162; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06162; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0031511; C:Mis6-Sim4 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR018565; Nkp2/Cnl2.
DR PANTHER; PTHR28064; PTHR28064; 2.
DR Pfam; PF09447; Cnl2_NKP2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..153
FT /note="Inner kinetochore subunit NKP2"
FT /id="PRO_0000096868"
FT COILED 86..128
FT /evidence="ECO:0000255"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 58..80
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 89..123
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:6QLF"
SQ SEQUENCE 153 AA; 17862 MW; 1445E11838649D70 CRC64;
MNSEQLLHNY VSDSLLTTLI SFQEFKQQLQ SYTSDEQQLQ HWYELLQARD ARVTSELEAR
IKQFFITLRS RLLRFLESEQ LSHSLSLETL IDALYKINDL LQQRLQILDD AIQEKTSELA
EFENMVRSPS AGDNAIPGLL QIIQSYINLL EEN
