DASH complex subunit DAD2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P36162 (DAD2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 99. 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 DAD2

Alternative name(s):
DUO1 and DAM1-interacting protein 2
Helper of ASK1 protein 1
Outer kinetochore protein DAD2

Gene names

Name:	DAD2
Synonyms:	HSK1
Ordered Locus Names:	YKR083C
ORF Names:	YKR403

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	133 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.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.6
Miscellaneous	Present with 279 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DASH complex DAD2 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Microtubule Nucleus
Domain	Coiled coil
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 mutant phenotype 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 Ref.5 Ref.9 Ref.8. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW mitotic spindle Inferred from direct assay PubMed 11756468. Source: SGD
Molecular_function	structural constituent of cytoskeleton Inferred from direct assay PubMed 11756468. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASK1	P35734	8	EBI-26515,EBI-26682

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 133

133

DASH complex subunit DAD2

PRO_0000211598

Regions

Coiled coil

1 – 51

Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P36162 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 82730D4AA5B66951
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FASTA

133

15,072

        10         20         30         40         50         60 
MDSIDEQIAI KRKELQSLQK ITSLTDGLKI QLTELNEQIK EMGMNADSVA QLMNNWDSII 

        70         80         90        100        110        120 
NNISQASLGL LQYAEGDYEI GPWKDSKKKE SEQSNETGLE AQENDKNDED NDEDEDLVPL 

       130 
PETMVRIRVD GNE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open reading frames." Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G., Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F. Yeast 10:231-245(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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]	"The mitotic spindle is required for loading of the DASH complex onto the kinetochore." Li Y., Bachant J.B., Alcasabas A.A., Wang Y., Qin J., Elledge S.J. Genes Dev. 16:183-197(2002) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF DASH COMPLEX.
[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 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.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z27116 Genomic DNA. Translation: CAA81634.1. Z28308 Genomic DNA. Translation: CAA82162.1. AY558397 Genomic DNA. Translation: AAS56723.1. BK006944 Genomic DNA. Translation: DAA09233.1.
PIR	S38161.
RefSeq	NP_013009.1. NM_001179873.1.
3D structure databases
ProteinModelPortal	P36162.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1927N.
IntAct	P36162. 7 interactions.
MINT	MINT-390119.
STRING	4932.YKR083C.
Proteomic databases
PaxDb	P36162.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKR083C; YKR083C; YKR083C.
GeneID	853958.
KEGG	sce:YKR083C.
Organism-specific databases
CYGD	YKR083c.
SGD	S000001791. DAD2.
Phylogenomic databases
eggNOG	NOG43922.
HOGENOM	HOG000001096.
KO	K11567.
OMA	YTENDYE.
OrthoDB	EOG4SBJ7Q.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32046-MONOMER.
Gene expression databases
Genevestigator	P36162.
GermOnline	YKR083C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013963. DASH_Dad2. [Graphical view]
Pfam	PF08654. DASH_Dad2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975377.

Entry information

Entry name

DAD2_YEAST

Accession

Primary (citable) accession number: P36162
Secondary accession number(s): D6VXE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 99 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 XI

Yeast (Saccharomyces cerevisiae) chromosome XI: 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

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents