DSN1_YEAST
ID DSN1_YEAST Reviewed; 576 AA.
AC P40568; D6VVU0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Kinetochore-associated protein DSN1;
GN Name=DSN1; OrderedLocusNames=YIR010W; ORFNames=YIB10W;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762303; DOI=10.1002/yea.320110109;
RA Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT "Nucleotide sequence and analysis of the centromeric region of yeast
RT chromosome IX.";
RL Yeast 11:61-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12455957; DOI=10.1128/ec.1.2.229-240.2002;
RA Euskirchen G.M.;
RT "Nnf1p, Dsn1p, Mtw1p, and Nsl1p: a new group of proteins important for
RT chromosome segregation in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 1:229-240(2002).
RN [5]
RP IDENTIFICATION IN THE MIND COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=14657030; DOI=10.1093/emboj/cdg636;
RA Scharfenberger M., Ortiz J., Grau N., Janke C., Schiebel E., Lechner J.;
RT "Nsl1p is essential for the establishment of bipolarity and the
RT localization of the Dam-Duo complex.";
RL EMBO J. 22:6584-6597(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NSL1.
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 [7]
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 [8]
RP IDENTIFICATION IN THE MIND COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=14602074; DOI=10.1016/s1534-5807(03)00322-8;
RA Pinsky B.A., Tatsutani S.Y., Collins K.A., Biggins S.;
RT "An Mtw1 complex promotes kinetochore biorientation that is monitored by
RT the Ipl1/Aurora protein kinase.";
RL Dev. Cell 5:735-745(2003).
RN [9]
RP IDENTIFICATION IN THE MIND COMPLEX, AND FUNCTION OF THE MIND COMPLEX.
RX PubMed=14633972; DOI=10.1101/gad.1144403;
RA De Wulf P., McAinsh A.D., Sorger P.K.;
RT "Hierarchical assembly of the budding yeast kinetochore from multiple
RT subcomplexes.";
RL Genes Dev. 17:2902-2921(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Acts as essential component of the kinetochore MIND complex,
CC which is required for the spindle checkpoint and kinetochore integrity.
CC MIND plays a role in establishing a bipolar spindle-kinetochore
CC interaction by joining kinetochore subunits contacting DNA to those
CC contacting microtubules. {ECO:0000269|PubMed:12455957,
CC ECO:0000269|PubMed:14633972}.
CC -!- SUBUNIT: Component of the MIND kinetochore complex, which is composed
CC of at least MTW1, NNF1, NSL1 and DSN1. Interacts with NSL1.
CC {ECO:0000269|PubMed:14602074, ECO:0000269|PubMed:14633972,
CC ECO:0000269|PubMed:14657030, ECO:0000269|PubMed:14690591}.
CC -!- INTERACTION:
CC P40568; P25651: CSM1; NbExp=3; IntAct=EBI-25398, EBI-22001;
CC P40568; Q12143: NSL1; NbExp=13; IntAct=EBI-25398, EBI-33666;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Associated with the kinetochore.
CC -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z37996; CAA86080.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08556.1; -; Genomic_DNA.
DR PIR; S48354; S48354.
DR RefSeq; NP_012275.3; NM_001179532.3.
DR PDB; 5T6J; X-ray; 1.75 A; C=560-572.
DR PDB; 6MJE; X-ray; 2.50 A; B/D/F/H=71-110.
DR PDBsum; 5T6J; -.
DR PDBsum; 6MJE; -.
DR AlphaFoldDB; P40568; -.
DR SMR; P40568; -.
DR BioGRID; 35002; 655.
DR ComplexPortal; CPX-1186; Nuclear MIS12/MIND complex.
DR DIP; DIP-4794N; -.
DR IntAct; P40568; 18.
DR MINT; P40568; -.
DR STRING; 4932.YIR010W; -.
DR iPTMnet; P40568; -.
DR MaxQB; P40568; -.
DR PaxDb; P40568; -.
DR PRIDE; P40568; -.
DR EnsemblFungi; YIR010W_mRNA; YIR010W; YIR010W.
DR GeneID; 854827; -.
DR KEGG; sce:YIR010W; -.
DR SGD; S000001449; DSN1.
DR VEuPathDB; FungiDB:YIR010W; -.
DR eggNOG; ENOG502QQ6A; Eukaryota.
DR HOGENOM; CLU_022497_1_0_1; -.
DR InParanoid; P40568; -.
DR OMA; PYMYYYP; -.
DR BioCyc; YEAST:G3O-31431-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P40568; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40568; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0000818; C:nuclear MIS12/MIND complex; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IGI:SGD.
DR InterPro; IPR013218; Dsn1/Mis13.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR PANTHER; PTHR14778; PTHR14778; 1.
DR Pfam; PF08202; MIS13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Kinetochore; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..576
FT /note="Kinetochore-associated protein DSN1"
FT /id="PRO_0000080024"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:6MJE"
FT HELIX 561..570
FT /evidence="ECO:0007829|PDB:5T6J"
SQ SEQUENCE 576 AA; 65692 MW; F859D3547378C072 CRC64;
MSLEPTQTVS GTPPMLHQRT HKQVYPLRME TIPILESDSK ATLQSNEPTQ KDEEETEYFE
NKQSVSNLSP DLKFKRHKNK HIQGFPTLGE RLDNLQDIKK AKRVENFNSS APIADDNHSG
DATANATANA TANATANVNA SAMPAPYMPY YYYYHPMNAP TPAMIPYPGS PMHSIMPNSS
LQPFYSQPTA AGGPDMTTPQ NISSSQQLLP APQLFPYGSF HQQQLQQPHY IQRTRERKKS
IGSQRGRRLS MLASQANGGS TIISPHKDIP EEDFYTVVGN ASFGKNLQIR QLFNWCLMRS
LHKLELKAKN QEEEGELEHL TKKSKLESTK AETDYVDPKR LAMVIIKEFV DDLKKDHIAI
DWEDEEKYED EDEEKILDNT ENYDDTELRQ LFQENDDDDD DDDEVDYSEI QRSRRKFSER
RKALPKEPKK LLPNSKNVEN TKNLSILTSK VNAIKNEVKE WAVTLDTSRP DLEWQELTSF
SSQPLEPLSD TEEPDLAIAD VETKLETKVD ELRYQSHILN SHSLALNEIT NSKVNKLNIE
TMRKISSETD DDHSQVINPQ QLLKGLSLSF SKKLDL
