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P53168 (DUO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.9 Ref.11

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.10

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore. 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 247246DASH complex subunit DUO1
PRO_0000215595

Regions

Coiled coil152 – 18029 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.12

Experimental info

Mutagenesis671E → K in DUO1-1; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with V-157. Ref.5
Mutagenesis1171A → T in DUO1-2; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with I-124. Ref.5
Mutagenesis1241M → I in DUO1-2; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with T-117. Ref.5
Mutagenesis1571A → V in DUO1-1; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with K-67. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P53168 [UniParc].

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

FASTA24727,473
        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' 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. expand/collapse author list , 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.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., 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]"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.
[10]"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.
[11]"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.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[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.
PIRS64065.
RefSeqNP_011454.1. NM_001180926.1.

3D structure databases

ProteinModelPortalP53168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33186. 162 interactions.
DIPDIP-1287N.
IntActP53168. 7 interactions.
MINTMINT-405719.
STRING4932.YGL061C.

Proteomic databases

MaxQBP53168.
PaxDbP53168.
PeptideAtlasP53168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL061C; YGL061C; YGL061C.
GeneID852819.
KEGGsce:YGL061C.

Organism-specific databases

CYGDYGL061c.
SGDS000003029. DUO1.

Phylogenomic databases

eggNOGNOG42829.
HOGENOMHOG000112294.
KOK11570.
OMAHEVCKST.
OrthoDBEOG74FFDB.

Enzyme and pathway databases

BioCycYEAST:G3O-30569-MONOMER.

Gene expression databases

GenevestigatorP53168.

Family and domain databases

InterProIPR013960. DASH_Duo1.
[Graphical view]
PfamPF08651. DASH_Duo1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972363.

Entry information

Entry nameDUO1_YEAST
AccessionPrimary (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: June 11, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families