DASH complex subunit DUO1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53168 (DUO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DASH complex subunit DUO1

Alternative name(s):
Death upon overproduction protein 1
Outer kinetochore protein DUO1

Gene names

Name:	DUO1
Ordered Locus Names:	YGL061C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5 Ref.8 Ref.10 Ref.12
Subunit structure	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. Ref.11
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › spindle. Chromosome › centromere › kinetochore. Note: Associates with the mitotic spindle and the kinetochore. Ref.5 Ref.6
Miscellaneous	Present with 996 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DASH complex DUO1 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Microtubule Nucleus
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic spindle organization in nucleus Inferred from physical interaction PubMed 11756468. Source: SGD regulation of microtubule polymerization or depolymerization Inferred from physical interaction Ref.8. Source: SGD
Cellular_component	DASH complex Inferred from direct assay PubMed 11799062 Ref.13 Ref.8. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW mitotic spindle Inferred from electronic annotation. Source: InterPro spindle microtubule Inferred from direct assay Ref.5. Source: SGD spindle pole body Inferred from direct assay Ref.5. Source: SGD
Molecular_function	structural constituent of cytoskeleton Inferred from physical interaction PubMed 11756468. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
DAD1	Q12248	4	EBI-23800,EBI-35662
DAM1	P53267	6	EBI-23800,EBI-23268
SPC34	P36131	3	EBI-23800,EBI-26401

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 247

247

DASH complex subunit DUO1

PRO_0000215595

Regions

Coiled coil

152 – 180

Potential

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Experimental info

Mutagenesis

E → K in DUO1-1; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with V-157. Ref.5

Mutagenesis

117

A → T in DUO1-2; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with I-124. Ref.5

Mutagenesis

124

M → I in DUO1-2; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with T-117. Ref.5

Mutagenesis

157

A → V in DUO1-1; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with K-67. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P53168 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 787F8AF869E3C978
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FASTA

247

27,473

        10         20         30         40         50         60 
MSEQSQLDDS TIDKLIPQIF NEMRSNLNNT TNKFPKSTGG GASDNISANS NSIRSFNSIT 

        70         80         90        100        110        120 
TQSLLKESES LDKITAMIKN VTAALKNNLP VYVNQVHEVC KSTNSILDSW INIHSQAGYI 

       130        140        150        160        170        180 
HKLMSDQTYL KLINDRLHNE NVNTNDEDGS TLHNVIALKK KEILDLRQKL ENRKGEKDAA 

       190        200        210        220        230        240 
PAKPPNQGLN PRYGVQSGRR PVPSAGISNN GRVRKTHVPA SKRPSGIPRV TNRWTKPTAS 


SSRKMFR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes." Feuermann M., de Montigny J., Potier S., Souciet J.-L. Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." 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. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Saccharomyces cerevisiae Duo1p and Dam1p, novel proteins involved in mitotic spindle function." Hofmann C., Cheeseman I.M., Goode B.L., McDonald K.L., Barnes G., Drubin D.G. J. Cell Biol. 143:1029-1040(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-67; ALA-117; MET-124 AND ALA-157.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Formation of a dynamic kinetochore-microtubule interface through assembly of the Dam1 ring complex." Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J., Drubin D.G., Nogales E., Barnes G. Mol. Cell 17:277-290(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, MASS SPECTROMETRY.
[10]	"The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends." Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E., Barnes G. Nature 440:565-569(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Molecular architecture of a kinetochore-microtubule attachment site." Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D. Nat. Cell Biol. 8:581-585(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[12]	"The Dam1 kinetochore complex harnesses microtubule dynamics to produce force and movement." Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N. Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"The yeast DASH complex forms closed rings on microtubules." Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C. Nat. Struct. Mol. Biol. 12:138-143(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z72583 Genomic DNA. Translation: CAA96764.1. AY558484 Genomic DNA. Translation: AAS56810.1. BK006941 Genomic DNA. Translation: DAA08041.1.
PIR	S64065.
RefSeq	NP_011454.1. NM_001180926.1.
3D structure databases
ProteinModelPortal	P53168.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1287N.
IntAct	P53168. 7 interactions.
MINT	MINT-405719.
STRING	4932.YGL061C.
Proteomic databases
PaxDb	P53168.
PeptideAtlas	P53168.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL061C; YGL061C; YGL061C.
GeneID	852819.
KEGG	sce:YGL061C.
Organism-specific databases
CYGD	YGL061c.
SGD	S000003029. DUO1.
Phylogenomic databases
eggNOG	NOG42829.
HOGENOM	HOG000112294.
KO	K11570.
OMA	HEVCKST.
OrthoDB	EOG48D455.
Gene expression databases
Genevestigator	P53168.
GermOnline	YGL061C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013960. DASH_Duo1. [Graphical view]
Pfam	PF08651. DASH_Duo1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972363.

Entry information

Entry name

DUO1_YEAST

Accession

Primary (citable) accession number: P53168
Secondary accession number(s): D6VU80

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents