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DASH complex subunit DAM1 (DUO1 and MPS1-interacting protein 1) (Kinetochore assembly protein DAM1) (Outer kinetochore protein DAM1)

 DAM1_YEAST              Reviewed;         343 AA.
P53267; D6VUP6; Q9P422;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
18-JUL-2018, entry version 141.
RecName: Full=DASH complex subunit DAM1;
AltName: Full=DUO1 and MPS1-interacting protein 1;
AltName: Full=Kinetochore assembly protein DAM1;
AltName: Full=Outer kinetochore protein DAM1;
Name=DAM1; OrderedLocusNames=YGR113W; ORFNames=G6153;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND KINETOCHORE FUNCTION.
PubMed=11149931; DOI=10.1083/jcb.152.1.197;
Cheeseman I.M., Enquist-Newman M., Mueller-Reichert T., Drubin D.G.,
Barnes G.;
"Mitotic spindle integrity and kinetochore function linked by the
Duo1p/Dam1p complex.";
J. Cell Biol. 152:197-212(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=8905931;
DOI=10.1002/(SICI)1097-0061(19960930)12:12<1273::AID-YEA21>3.0.CO;2-J;
Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
Schreer A., Schaefer B., Zimmermann M., Wolf K.;
"The sequence of a 23.4 kb segment on the right arm of chromosome VII
from Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57
genes, a Ty3 element and 11 new open reading frames.";
Yeast 12:1273-1277(1996).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9817759; DOI=10.1083/jcb.143.4.1029;
Hofmann C., Cheeseman I.M., Goode B.L., McDonald K.L., Barnes G.,
Drubin D.G.;
"Saccharomyces cerevisiae Duo1p and Dam1p, novel proteins involved in
mitotic spindle function.";
J. Cell Biol. 143:1029-1040(1998).
[6]
MUTAGENESIS OF CYS-111.
PubMed=10397771; DOI=10.1091/mbc.10.7.2377;
Jones M.H., Bachant J.B., Castillo A.R., Giddings T.H. Jr., Winey M.;
"Yeast Dam1p is required to maintain spindle integrity during mitosis
and interacts with the Mps1p kinase.";
Mol. Biol. Cell 10:2377-2391(1999).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=11724818; DOI=10.1083/jcb.200105029;
Kang J.-S., Cheeseman I.M., Kallstrom G., Velmurugan S., Barnes G.,
Chan C.S.M.;
"Functional cooperation of Dam1, Ipl1, and the inner centromere
protein (INCENP)-related protein Sli15 during chromosome
segregation.";
J. Cell Biol. 155:763-774(2001).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11698664; DOI=10.1073/pnas.241417098;
Jones M.H., He X., Giddings T.H. Jr., Winey M.;
"Yeast Dam1p has a role at the kinetochore in assembly of the mitotic
spindle.";
Proc. Natl. Acad. Sci. U.S.A. 98:13675-13680(2001).
[9]
PHOSPHORYLATION AT SER-20; SER-257; SER-265 AND SER-292.
PubMed=12408861; DOI=10.1016/S0092-8674(02)00973-X;
Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,
Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
"Phospho-regulation of kinetochore-microtubule attachments by the
Aurora kinase Ipl1p.";
Cell 111:163-172(2002).
[10]
INTERACTION WITH SPC34 AND TID3.
PubMed=12925767; DOI=10.1091/mbc.E02-11-0765;
Shang C., Hazbun T.R., Cheeseman I.M., Aranda J., Fields S.,
Drubin D.G., Barnes G.;
"Kinetochore protein interactions and their regulation by the Aurora
kinase Ipl1p.";
Mol. Biol. Cell 14:3342-3355(2003).
[11]
FUNCTION.
PubMed=15664196; DOI=10.1016/j.molcel.2004.12.019;
Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J.,
Drubin D.G., Nogales E., Barnes G.;
"Formation of a dynamic kinetochore-microtubule interface through
assembly of the Dam1 ring complex.";
Mol. Cell 17:277-290(2005).
[12]
FUNCTION.
PubMed=16415853; DOI=10.1038/nature04409;
Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E.,
Barnes G.;
"The Dam1 kinetochore ring complex moves processively on
depolymerizing microtubule ends.";
Nature 440:565-569(2006).
[13]
SUBUNIT.
PubMed=16715078; DOI=10.1038/ncb1414;
Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
"Molecular architecture of a kinetochore-microtubule attachment
site.";
Nat. Cell Biol. 8:581-585(2006).
[14]
FUNCTION.
PubMed=16777964; DOI=10.1073/pnas.0602249103;
Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.;
"The Dam1 kinetochore complex harnesses microtubule dynamics to
produce force and movement.";
Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-292, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.
PubMed=15640796; DOI=10.1038/nsmb896;
Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.;
"The yeast DASH complex forms closed rings on microtubules.";
Nat. Struct. Mol. Biol. 12:138-143(2005).
-!- FUNCTION: Component of the DASH complex, a microtubule-binding
subcomplex of the outer kinetochore that is essential for proper
chromosome segregation. The DASH complex mediates the formation
and maintenance of bipolar kinetochore-microtubule attachments by
forming closed rings around spindle microtubules and establishing
interactions with proteins from the central kinetochore. The DASH
ring complex may both stabilize microtubules during chromosome
attachment in anaphase A, and allow the chromosome to remain
attached to the depolymerizing microtubule in anaphase B.
Microtubule depolymerization proceeds by protofilament splaying
and induces the kinetochore-attached ring to slide longitudinally,
thereby helping to transduce depolymerization energy into pulling
forces to disjoin chromatids. {ECO:0000269|PubMed:11698664,
ECO:0000269|PubMed:11724818, ECO:0000269|PubMed:15664196,
ECO:0000269|PubMed:16415853, ECO:0000269|PubMed:16777964,
ECO:0000269|PubMed:9817759}.
-!- SUBUNIT: The DASH complex is an approximately 210 kDa
heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4,
DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry
of one copy of each subunit. DASH oligomerizes into a 50 nm ring
composed of about 16 molecules that encircles the microtubule.
Integrity of the complex and interactions with central kinetochore
proteins are regulated by the spindle assembly checkpoint kinase
IPL1. Interacts with TID3. {ECO:0000269|PubMed:12925767,
ECO:0000269|PubMed:16715078}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-23268, EBI-23268;
P35734:ASK1; NbExp=8; IntAct=EBI-23268, EBI-26682;
P40013:BIM1; NbExp=2; IntAct=EBI-23268, EBI-3614;
P32504:CBF2; NbExp=2; IntAct=EBI-23268, EBI-4069;
P36012:CSE4; NbExp=3; IntAct=EBI-23268, EBI-5182;
P35203:CTF13; NbExp=2; IntAct=EBI-23268, EBI-4085;
Q02732:CTF19; NbExp=2; IntAct=EBI-23268, EBI-5199;
Q12248:DAD1; NbExp=4; IntAct=EBI-23268, EBI-35662;
P36162:DAD2; NbExp=2; IntAct=EBI-23268, EBI-26515;
P53168:DUO1; NbExp=6; IntAct=EBI-23268, EBI-23800;
P40460:NDC80; NbExp=4; IntAct=EBI-23268, EBI-25247;
P53298:OKP1; NbExp=2; IntAct=EBI-23268, EBI-23429;
P38283:SLI15; NbExp=2; IntAct=EBI-23268, EBI-20842;
Q03954:SPC19; NbExp=3; IntAct=EBI-23268, EBI-38809;
P36131:SPC34; NbExp=4; IntAct=EBI-23268, EBI-26401;
P46675:STU2; NbExp=3; IntAct=EBI-23268, EBI-18471;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
Chromosome, centromere, kinetochore. Note=Associates with the
mitotic spindle and the kinetochore.
-!- SIMILARITY: Belongs to the DASH complex DAM1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA97121.1; Type=Frameshift; Positions=292; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF280542; AAF82130.1; -; Genomic_DNA.
EMBL; Z72898; CAA97121.1; ALT_FRAME; Genomic_DNA.
EMBL; BK006941; DAA08207.1; -; Genomic_DNA.
PIR; S64421; S64421.
RefSeq; NP_011628.4; NM_001181242.3.
ProteinModelPortal; P53267; -.
SMR; P53267; -.
BioGrid; 33360; 712.
ComplexPortal; CPX-1041; DASH complex.
DIP; DIP-1286N; -.
IntAct; P53267; 51.
MINT; P53267; -.
STRING; 4932.YGR113W; -.
iPTMnet; P53267; -.
MaxQB; P53267; -.
PaxDb; P53267; -.
PRIDE; P53267; -.
EnsemblFungi; YGR113W; YGR113W; YGR113W.
GeneID; 853010; -.
KEGG; sce:YGR113W; -.
EuPathDB; FungiDB:YGR113W; -.
SGD; S000003345; DAM1.
HOGENOM; HOG000000932; -.
InParanoid; P53267; -.
KO; K02307; -.
OMA; LLYGLMC; -.
OrthoDB; EOG092C5P0B; -.
BioCyc; YEAST:G3O-30822-MONOMER; -.
PRO; PR:P53267; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0042729; C:DASH complex; IDA:SGD.
GO; GO:1990537; C:mitotic spindle polar microtubule; IBA:GO_Central.
GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:1990758; P:mitotic sister chromatid biorientation; IBA:GO_Central.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
InterPro; IPR013962; DASH_Dam1.
Pfam; PF08653; DASH_Dam1; 1.
ProDom; PD398536; DASH_Dam1; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
Chromosome partition; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 343 DASH complex subunit DAM1.
/FTId=PRO_0000127663.
COILED 125 158 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 20 20 Phosphoserine; by IPL1.
{ECO:0000269|PubMed:12408861}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 257 257 Phosphoserine; by IPL1.
{ECO:0000269|PubMed:12408861}.
MOD_RES 265 265 Phosphoserine; by IPL1.
{ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:12408861}.
MOD_RES 292 292 Phosphoserine; by IPL1.
{ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:12408861}.
MUTAGEN 111 111 C->Y: In DAM1-1; produces abnormal
spindles resulting in growth arrest at 34
degrees Celsius.
{ECO:0000269|PubMed:10397771}.
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


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