NKP1_YEAST
ID NKP1_YEAST Reviewed; 238 AA.
AC Q12493; D6VT17;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Inner kinetochore subunit NKP1 {ECO:0000305};
DE AltName: Full=Constitutive centromere-associated network protein NKP1 {ECO:0000305};
DE AltName: Full=Non-essential kinetochore protein 1;
GN Name=NKP1; OrderedLocusNames=YDR383C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF CENTRAL KINETOCHORE
RP COMPLEX, AND 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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:Q6CPR4,
CC ECO:0000269|PubMed:22561346}.
CC -!- INTERACTION:
CC Q12493; Q06162: NKP2; NbExp=3; IntAct=EBI-35840, EBI-34256;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12408861}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12408861,
CC ECO:0000269|PubMed:29046335}. Note=Associated with kinetochores.
CC -!- SIMILARITY: Belongs to the NKP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64819.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB64825.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U28373; AAB64819.1; ALT_INIT; Genomic_DNA.
DR EMBL; U32274; AAB64825.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA12227.1; -; Genomic_DNA.
DR PIR; S61178; S61178.
DR RefSeq; NP_010671.4; NM_001180691.3.
DR PDB; 6NUW; EM; 4.25 A; G=1-238.
DR PDB; 6QLD; EM; 4.15 A; Y=2-238.
DR PDB; 6QLE; EM; 3.55 A; Y=1-238.
DR PDB; 6QLF; EM; 3.45 A; Y=1-238.
DR PDBsum; 6NUW; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6QLF; -.
DR AlphaFoldDB; Q12493; -.
DR SMR; Q12493; -.
DR BioGRID; 32444; 77.
DR ComplexPortal; CPX-1156; Central kinetochore CTF19 complex.
DR DIP; DIP-1940N; -.
DR IntAct; Q12493; 10.
DR MINT; Q12493; -.
DR STRING; 4932.YDR383C; -.
DR iPTMnet; Q12493; -.
DR MaxQB; Q12493; -.
DR PaxDb; Q12493; -.
DR PRIDE; Q12493; -.
DR EnsemblFungi; YDR383C_mRNA; YDR383C; YDR383C.
DR GeneID; 851991; -.
DR KEGG; sce:YDR383C; -.
DR SGD; S000002791; NKP1.
DR VEuPathDB; FungiDB:YDR383C; -.
DR eggNOG; ENOG502S64F; Eukaryota.
DR HOGENOM; CLU_101503_0_0_1; -.
DR InParanoid; Q12493; -.
DR OMA; YELENEW; -.
DR BioCyc; YEAST:G3O-29931-MON; -.
DR ChiTaRS; NKP1; yeast.
DR PRO; PR:Q12493; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12493; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Kinetochore; Meiosis; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..238
FT /note="Inner kinetochore subunit NKP1"
FT /id="PRO_0000096867"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 16..21
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 49..54
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 58..81
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 137..185
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:6QLF"
SQ SEQUENCE 238 AA; 26976 MW; A2BE651F72E76B54 CRC64;
MTDTYNSISN FIENELTALL SSDDYLMDDL AGELPNEVCR LLKAQVIEKR KDAMSRGKQD
LLSKEIYDNE SELRASQSQQ IMELVGDIPK YSLGSELRNR VEGEPQSTSI ERLIEDVLKL
PQMEVADEEE VEVENDLKVL SEYSNLRKDL ILKCQALQIG ESKLSDILSQ TNSINSLTTS
IKEASEDDDI SEYFATYNGK LVVALEEMKL LLEEAVKTFG NSPEKREKIK KILSELKK
