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P40460

- NDC80_YEAST

UniProt

P40460 - NDC80_YEAST

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Protein
Kinetochore protein NDC80
Gene
TID3, HEC1, NDC80, YIL144W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a component of the essential kinetochore-associated NDC80 complex, which is involved in chromosome segregation and spindle checkpoint activity.4 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. protein binding Source: IntAct
  3. structural constituent of cytoskeleton Source: SGD
Complete GO annotation...

GO - Biological processi

  1. chromosome segregation Source: SGD
  2. microtubule nucleation Source: SGD
  3. mitotic nuclear division Source: UniProtKB-KW
  4. protein localization to kinetochore Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BioCyciYEAST:G3O-31394-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinetochore protein NDC80
Alternative name(s):
Protein TID3
Gene namesi
Name:TID3
Synonyms:HEC1, NDC80
Ordered Locus Names:YIL144W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL144w.
SGDiS000001406. TID3.

Subcellular locationi

Nucleus. Chromosomecentromerekinetochore
Note: Associated with kinetochores.5 Publications

GO - Cellular componenti

  1. Ndc80 complex Source: SGD
  2. condensed nuclear chromosome kinetochore Source: SGD
  3. condensed nuclear chromosome, centromeric region Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011S → A: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691Kinetochore protein NDC80
PRO_0000202958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphothreonine1 Publication
Modified residuei248 – 2481Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40460.
PaxDbiP40460.

Expressioni

Gene expression databases

GenevestigatoriP40460.

Interactioni

Subunit structurei

Component of the NDC80 complex, which consists of TID3/NDC80, NUF2, SPC24 and SPC25. The NDC80 complex is formed by two subcomplexes, TID3/NDC80-NUF2 and SPC24-SPC25, which are joined end-to-end through their coiled-coil domains. It has a rod-like structure with a length of 570 Angstroms and globular domains at either end. The TID3/NDC80-NUF2 globular domains are probably directed to microtubules, the SPC24-SPC25 globular domains to the centromere. TID3 probably interacts with SMC1 and SMC2. Also interacts with KIN3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-25247,EBI-25247
DAM1P532674EBI-25247,EBI-23268
MPS1P541994EBI-25247,EBI-11224
NUF2P3389516EBI-25247,EBI-12377
SPC105P531482EBI-25247,EBI-23870
SPC24Q0447719EBI-25247,EBI-27228
SPC25P4001413EBI-25247,EBI-22458

Protein-protein interaction databases

BioGridi34848. 93 interactions.
DIPiDIP-818N.
IntActiP40460. 39 interactions.
MINTiMINT-408680.
STRINGi4932.YIL144W.

Structurei

3D structure databases

ProteinModelPortaliP40460.
SMRiP40460. Positions 114-362.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili376 – 44671 Reviewed prediction
Add
BLAST
Coiled coili522 – 686165 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the NDC80/HEC1 family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5185.
GeneTreeiENSGT00390000018386.
HOGENOMiHOG000113749.
KOiK11547.
OMAiREYEECM.
OrthoDBiEOG7034SB.

Family and domain databases

InterProiIPR005550. Kinetochore_Ndc80.
[Graphical view]
PANTHERiPTHR10643. PTHR10643. 1 hit.
PfamiPF03801. Ndc80_HEC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40460-1 [UniParc]FASTAAdd to Basket

« Hide

MQSSTSTDQH VLHHMDPHRF TSQIPTATSS QLRRRNSTNQ GLTDMINKSI    50
ARNTISGTGI PTGGINKNKR TRSTVAGGTN GTALALNDKS NSRNSVSRLS 100
INQLGSLQQH LSNRDPRPLR DKNFQSAIQE EIYDYLKKNK FDIETNHPIS 150
IKFLKQPTQK GFIIIFKWLY LRLDPGYGFT KSIENEIYQI LKNLRYPFLE 200
SINKSQISAV GGSNWHKFLG MLHWMVRTNI KLDMCLNKVD RSLINQNTQE 250
ITILSQPLKT LDEQDQRQER YELMVEKLLI DYFTESYKSF LKLEDNYEPS 300
MQELKLGFEK FVHIINTDIA NLQTQNDNLY EKYQEVMKIS QKIKTTREKW 350
KALKSDSNKY ENYVNAMKQK SQEWPGKLEK MKSECELKEE EIKALQSNIS 400
ELHKILRKKG ISTEQFELQN QEREKLTREL DKINIQSDKL TSSIKSRKLE 450
AEGIFKSLLD TLRQYDSSIQ NLTRSRSQLG HNVNDSSLKI NISENLLDRD 500
FHEGISYEQL FPKGSGINES IKKSILKLND EIQERIKTIE KDNITLEKDI 550
KNLKHDINEK TQINEKLELE LSEANSKFEL SKQENERLLV AQRIEIEKME 600
KKINDSNLLM KTKISDAEEL VTSTELKLEE LKVDLNRKRY KLHQQVIHVI 650
DITSKFKINI QSSLENSENE LGNVIEELRN LEFETEHNVT N 691
Length:691
Mass (Da):80,487
Last modified:February 1, 1995 - v1
Checksum:i7DBC492227A80093
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38059 Genomic DNA. Translation: CAA86134.1.
BK006942 Genomic DNA. Translation: DAA08409.1.
PIRiS48390.
RefSeqiNP_012122.3. NM_001179492.3.

Genome annotation databases

EnsemblFungiiYIL144W; YIL144W; YIL144W.
GeneIDi854662.
KEGGisce:YIL144W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38059 Genomic DNA. Translation: CAA86134.1 .
BK006942 Genomic DNA. Translation: DAA08409.1 .
PIRi S48390.
RefSeqi NP_012122.3. NM_001179492.3.

3D structure databases

ProteinModelPortali P40460.
SMRi P40460. Positions 114-362.
ModBasei Search...

Protein-protein interaction databases

BioGridi 34848. 93 interactions.
DIPi DIP-818N.
IntActi P40460. 39 interactions.
MINTi MINT-408680.
STRINGi 4932.YIL144W.

Proteomic databases

MaxQBi P40460.
PaxDbi P40460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIL144W ; YIL144W ; YIL144W .
GeneIDi 854662.
KEGGi sce:YIL144W.

Organism-specific databases

CYGDi YIL144w.
SGDi S000001406. TID3.

Phylogenomic databases

eggNOGi COG5185.
GeneTreei ENSGT00390000018386.
HOGENOMi HOG000113749.
KOi K11547.
OMAi REYEECM.
OrthoDBi EOG7034SB.

Enzyme and pathway databases

BioCyci YEAST:G3O-31394-MONOMER.

Miscellaneous databases

NextBioi 977235.
PROi P40460.

Gene expression databases

Genevestigatori P40460.

Family and domain databases

InterProi IPR005550. Kinetochore_Ndc80.
[Graphical view ]
PANTHERi PTHR10643. PTHR10643. 1 hit.
Pfami PF03801. Ndc80_HEC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Components of the yeast spindle and spindle pole body."
    Rout M.P., Kilmartin J.V.
    J. Cell Biol. 111:1913-1927(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry."
    Wigge P.A., Jensen O.N., Holmes S., Soues S., Mann M., Kilmartin J.V.
    J. Cell Biol. 141:967-977(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION.
  5. "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins."
    Zheng L., Chen Y., Lee W.-H.
    Mol. Cell. Biol. 19:5417-5428(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMC1 AND SMC2.
  6. "The budding yeast proteins Spc24p and Spc25p interact with Ndc80p and Nuf2p at the kinetochore and are important for kinetochore clustering and checkpoint control."
    Janke C., Ortiz J., Lechner J., Shevchenko A., Shevchenko A., Magiera M.M., Schramm C., Schiebel E.
    EMBO J. 20:777-791(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SPC24 AND SPC25.
  7. "The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation."
    Wigge P.A., Kilmartin J.V.
    J. Cell Biol. 152:349-360(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE NDC80 COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NDC80 COMPLEX.
  8. "Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinase is essential for faithful chromosome segregation."
    Chen Y., Riley D.J., Zheng L., Chen P.-L., Lee W.-H.
    J. Biol. Chem. 277:49408-49416(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIN3, MUTAGENESIS OF SER-201.
  9. "Spc24 interacts with Mps2 and is required for chromosome segregation, but is not implicated in spindle pole body duplication."
    Le Masson I., Saveanu C., Chevalier A., Namane A., Gobin R., Fromont-Racine M., Jacquier A., Mann C.
    Mol. Microbiol. 43:1431-1443(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPC24 AND SPC25.
  10. "The highly conserved Ndc80 complex is required for kinetochore assembly, chromosome congression, and spindle checkpoint activity."
    McCleland M.L., Gardner R.D., Kallio M.J., Daum J.R., Gorbsky G.J., Burke D.J., Stukenberg P.T.
    Genes Dev. 17:101-114(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE NDC80 COMPLEX.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "The fission yeast kinetochore component Spc7 associates with the EB1 family member Mal3 and is required for kinetochore-spindle association."
    Kerres A., Vietmeier-Decker C., Ortiz J., Karig I., Beuter C., Hegemann J., Lechner J., Fleig U.
    Mol. Biol. Cell 15:5255-5267(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NDC80 COMPLEX.
  13. "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 THR-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Molecular organization of the Ndc80 complex, an essential kinetochore component."
    Wei R.R., Sorger P.K., Harrison S.C.
    Proc. Natl. Acad. Sci. U.S.A. 102:5363-5367(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF THE NDC80 COMPLEX.

Entry informationi

Entry nameiNDC80_YEAST
AccessioniPrimary (citable) accession number: P40460
Secondary accession number(s): D6VVE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1160 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

Similar proteinsi