DAM1_YEAST
ID DAM1_YEAST Reviewed; 343 AA.
AC P53267; D6VUP6; Q9P422;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=DASH complex subunit DAM1;
DE AltName: Full=DUO1 and MPS1-interacting protein 1;
DE AltName: Full=Kinetochore assembly protein DAM1;
DE AltName: Full=Outer kinetochore protein DAM1;
GN Name=DAM1; OrderedLocusNames=YGR113W; ORFNames=G6153;
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 KINETOCHORE FUNCTION.
RX PubMed=11149931; DOI=10.1083/jcb.152.1.197;
RA Cheeseman I.M., Enquist-Newman M., Mueller-Reichert T., Drubin D.G.,
RA Barnes G.;
RT "Mitotic spindle integrity and kinetochore function linked by the
RT Duo1p/Dam1p complex.";
RL J. Cell Biol. 152:197-212(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8905931;
RX DOI=10.1002/(sici)1097-0061(19960930)12:12<1273::aid-yea21>3.0.co;2-j;
RA Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
RA Schreer A., Schaefer B., Zimmermann M., Wolf K.;
RT "The sequence of a 23.4 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3
RT element and 11 new open reading frames.";
RL Yeast 12:1273-1277(1996).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9817759; DOI=10.1083/jcb.143.4.1029;
RA Hofmann C., Cheeseman I.M., Goode B.L., McDonald K.L., Barnes G.,
RA Drubin D.G.;
RT "Saccharomyces cerevisiae Duo1p and Dam1p, novel proteins involved in
RT mitotic spindle function.";
RL J. Cell Biol. 143:1029-1040(1998).
RN [6]
RP MUTAGENESIS OF CYS-111.
RX PubMed=10397771; DOI=10.1091/mbc.10.7.2377;
RA Jones M.H., Bachant J.B., Castillo A.R., Giddings T.H. Jr., Winey M.;
RT "Yeast Dam1p is required to maintain spindle integrity during mitosis and
RT interacts with the Mps1p kinase.";
RL Mol. Biol. Cell 10:2377-2391(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=11724818; DOI=10.1083/jcb.200105029;
RA Kang J.-S., Cheeseman I.M., Kallstrom G., Velmurugan S., Barnes G.,
RA Chan C.S.M.;
RT "Functional cooperation of Dam1, Ipl1, and the inner centromere protein
RT (INCENP)-related protein Sli15 during chromosome segregation.";
RL J. Cell Biol. 155:763-774(2001).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11698664; DOI=10.1073/pnas.241417098;
RA Jones M.H., He X., Giddings T.H. Jr., Winey M.;
RT "Yeast Dam1p has a role at the kinetochore in assembly of the mitotic
RT spindle.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13675-13680(2001).
RN [9]
RP PHOSPHORYLATION AT SER-20; SER-257; SER-265 AND SER-292.
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 [10]
RP INTERACTION WITH SPC34 AND TID3.
RX PubMed=12925767; DOI=10.1091/mbc.e02-11-0765;
RA Shang C., Hazbun T.R., Cheeseman I.M., Aranda J., Fields S., Drubin D.G.,
RA Barnes G.;
RT "Kinetochore protein interactions and their regulation by the Aurora kinase
RT Ipl1p.";
RL Mol. Biol. Cell 14:3342-3355(2003).
RN [11]
RP FUNCTION.
RX PubMed=15664196; DOI=10.1016/j.molcel.2004.12.019;
RA Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J.,
RA Drubin D.G., Nogales E., Barnes G.;
RT "Formation of a dynamic kinetochore-microtubule interface through assembly
RT of the Dam1 ring complex.";
RL Mol. Cell 17:277-290(2005).
RN [12]
RP FUNCTION.
RX PubMed=16415853; DOI=10.1038/nature04409;
RA Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E.,
RA Barnes G.;
RT "The Dam1 kinetochore ring complex moves processively on depolymerizing
RT microtubule ends.";
RL Nature 440:565-569(2006).
RN [13]
RP SUBUNIT.
RX PubMed=16715078; DOI=10.1038/ncb1414;
RA Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
RT "Molecular architecture of a kinetochore-microtubule attachment site.";
RL Nat. Cell Biol. 8:581-585(2006).
RN [14]
RP FUNCTION.
RX PubMed=16777964; DOI=10.1073/pnas.0602249103;
RA Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.;
RT "The Dam1 kinetochore complex harnesses microtubule dynamics to produce
RT force and movement.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-292, AND
RP IDENTIFICATION BY 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).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.
RX PubMed=15640796; DOI=10.1038/nsmb896;
RA Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.;
RT "The yeast DASH complex forms closed rings on microtubules.";
RL Nat. Struct. Mol. Biol. 12:138-143(2005).
CC -!- FUNCTION: Component of the DASH complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation. The DASH complex mediates the formation and
CC maintenance of bipolar kinetochore-microtubule attachments by forming
CC closed rings around spindle microtubules and establishing interactions
CC with proteins from the central kinetochore. The DASH ring complex may
CC both stabilize microtubules during chromosome attachment in anaphase A,
CC and allow the chromosome to remain attached to the depolymerizing
CC microtubule in anaphase B. Microtubule depolymerization proceeds by
CC protofilament splaying and induces the kinetochore-attached ring to
CC slide longitudinally, thereby helping to transduce depolymerization
CC energy into pulling forces to disjoin chromatids.
CC {ECO:0000269|PubMed:11698664, ECO:0000269|PubMed:11724818,
CC ECO:0000269|PubMed:15664196, ECO:0000269|PubMed:16415853,
CC ECO:0000269|PubMed:16777964, ECO:0000269|PubMed:9817759}.
CC -!- SUBUNIT: The DASH complex is an approximately 210 kDa heterodecamer,
CC which consists of ASK1, DAD1, DAD2, DAD3, DAD4, DAM1, DUO1, HSK3, SPC19
CC and SPC34, with an apparent stoichiometry of one copy of each subunit.
CC DASH oligomerizes into a 50 nm ring composed of about 16 molecules that
CC encircles the microtubule. Integrity of the complex and interactions
CC with central kinetochore proteins are regulated by the spindle assembly
CC checkpoint kinase IPL1. Interacts with TID3.
CC {ECO:0000269|PubMed:12925767, ECO:0000269|PubMed:16715078}.
CC -!- INTERACTION:
CC P53267; P40013: BIM1; NbExp=2; IntAct=EBI-23268, EBI-3614;
CC P53267; P32504: CBF2; NbExp=2; IntAct=EBI-23268, EBI-4069;
CC P53267; P36012: CSE4; NbExp=2; IntAct=EBI-23268, EBI-5182;
CC P53267; P35203: CTF13; NbExp=2; IntAct=EBI-23268, EBI-4085;
CC P53267; Q02732: CTF19; NbExp=2; IntAct=EBI-23268, EBI-5199;
CC P53267; Q12248: DAD1; NbExp=4; IntAct=EBI-23268, EBI-35662;
CC P53267; P53267: DAM1; NbExp=2; IntAct=EBI-23268, EBI-23268;
CC P53267; P53168: DUO1; NbExp=6; IntAct=EBI-23268, EBI-23800;
CC P53267; P40460: NDC80; NbExp=4; IntAct=EBI-23268, EBI-25247;
CC P53267; P53298: OKP1; NbExp=2; IntAct=EBI-23268, EBI-23429;
CC P53267; P38283: SLI15; NbExp=2; IntAct=EBI-23268, EBI-20842;
CC P53267; P36131: SPC34; NbExp=4; IntAct=EBI-23268, EBI-26401;
CC P53267; P46675: STU2; NbExp=3; IntAct=EBI-23268, EBI-18471;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Chromosome, centromere, kinetochore. Note=Associates with the mitotic
CC spindle and the kinetochore.
CC -!- SIMILARITY: Belongs to the DASH complex DAM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA97121.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF280542; AAF82130.1; -; Genomic_DNA.
DR EMBL; Z72898; CAA97121.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006941; DAA08207.1; -; Genomic_DNA.
DR PIR; S64421; S64421.
DR RefSeq; NP_011628.4; NM_001181242.3.
DR AlphaFoldDB; P53267; -.
DR SMR; P53267; -.
DR BioGRID; 33360; 718.
DR ComplexPortal; CPX-1041; DASH complex.
DR DIP; DIP-1286N; -.
DR IntAct; P53267; 47.
DR MINT; P53267; -.
DR STRING; 4932.YGR113W; -.
DR iPTMnet; P53267; -.
DR MaxQB; P53267; -.
DR PaxDb; P53267; -.
DR PRIDE; P53267; -.
DR EnsemblFungi; YGR113W_mRNA; YGR113W; YGR113W.
DR GeneID; 853010; -.
DR KEGG; sce:YGR113W; -.
DR SGD; S000003345; DAM1.
DR VEuPathDB; FungiDB:YGR113W; -.
DR eggNOG; ENOG502S08R; Eukaryota.
DR HOGENOM; CLU_065404_0_0_1; -.
DR InParanoid; P53267; -.
DR OMA; LYGLMCN; -.
DR BioCyc; YEAST:G3O-30822-MON; -.
DR PRO; PR:P53267; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53267; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IDA:SGD.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:1990537; C:mitotic spindle polar microtubule; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IDA:ComplexPortal.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IDA:SGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
DR InterPro; IPR013962; DASH_Dam1.
DR PANTHER; PTHR28113; PTHR28113; 1.
DR Pfam; PF08653; DASH_Dam1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..343
FT /note="DASH complex subunit DAM1"
FT /id="PRO_0000127663"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..158
FT /evidence="ECO:0000255"
FT COMPBIAS 13..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 20
FT /note="Phosphoserine; by IPL1"
FT /evidence="ECO:0000269|PubMed:12408861"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 257
FT /note="Phosphoserine; by IPL1"
FT /evidence="ECO:0000269|PubMed:12408861"
FT MOD_RES 265
FT /note="Phosphoserine; by IPL1"
FT /evidence="ECO:0000269|PubMed:12408861,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 292
FT /note="Phosphoserine; by IPL1"
FT /evidence="ECO:0000269|PubMed:12408861,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 111
FT /note="C->Y: In DAM1-1; produces abnormal spindles
FT resulting in growth arrest at 34 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:10397771"
SQ SEQUENCE 343 AA; 38422 MW; F02DB6EE09BC2284 CRC64;
MSEDKAKLGT TRSATEYRLS IGSAPTSRRS SMGESSSLMK FADQEGLTSS VGEYNENTIQ
QLLLPKIREL SDSIITLDSN FTRLNFIHES LADLNESLGS LLYGIMSNSW CVEFSQAPHD
IQDDLIAIKQ LKSLEDEKNN LVMELSNMER GIKRKKDEQG ENDLAKASQN KQFNQPLFPS
SQVRKYRSYD NRDKRKPSKI GNNLQVENEE DYEDDTSSEA SFVLNPTNIG MSKSSQGHVT
KTTRLNNNTN SKLRRKSILH TIRNSIASGA DLPIENDNVV NLGDLHPNNR ISLGSGAARV
VNGPVTKNRN SMFSGRAERK PTESRHSVAK KTEKKINTRP PFR
