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Protein

Monopolin complex subunit LRS4

Gene

LRS4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Involved in rDNA silencing.3 Publications

GO - Biological processi

  1. chromatin silencing at rDNA Source: SGD
  2. homologous chromosome segregation Source: SGD
  3. protein localization to nucleolar rDNA repeats Source: SGD
  4. rDNA condensation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Meiosis

Enzyme and pathway databases

BioCyciYEAST:G3O-29973-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Monopolin complex subunit LRS4
Alternative name(s):
Loss of rDNA silencing protein 4
Gene namesi
Name:LRS4
Ordered Locus Names:YDR439W
ORF Names:D9461.25
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR439w.
SGDiS000002847. LRS4.

Subcellular locationi

Nucleusnucleolus. Chromosomecentromere
Note: Transiently released from the nucleolus and localized to the centromere regions during late pachytene. This relocation is CDC5 dependent.

GO - Cellular componenti

  1. monopolin complex Source: SGD
  2. nucleolus Source: SGD
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Monopolin complex subunit LRS4PRO_0000257808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei230 – 2301Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by CDC5. This phosphorylation is required for the location to the kinetochores during late pachytene.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04087.
PaxDbiQ04087.

Expressioni

Gene expression databases

GenevestigatoriQ04087.

Interactioni

Subunit structurei

Component of the monopolin complex composed of at least CSM1, LRS4 and MAM1. The complex associates with the kinetochore.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC5P325626EBI-32189,EBI-4440
CDC7P062435EBI-32189,EBI-4451
CSM1P2565116EBI-32189,EBI-22001

Protein-protein interaction databases

BioGridi32495. 359 interactions.
DIPiDIP-1416N.
IntActiQ04087. 14 interactions.
MINTiMINT-391498.
STRINGi4932.YDR439W.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N7NX-ray3.90E/F1-102[»]
ProteinModelPortaliQ04087.
SMRiQ04087. Positions 3-33.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04087.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili46 – 11873Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG72052.
InParanoidiQ04087.
KOiK12775.
OMAiMAHENER.
OrthoDBiEOG7673QD.

Family and domain databases

InterProiIPR018479. Lrs4/Mde4.
[Graphical view]
PfamiPF10422. LRS4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLLQLLSN YYKAKLDSER IYNEYVQSQY EFASLDKLNN NKGDPKKVVD
60 70 80 90 100
ETLFLQRQIA QLNKQLQLSF QENEKLLSVQ KNQKALYQSK LSSKDAFIDD
110 120 130 140 150
LKLKLKVEQI SVDKHNKERT PSTGRDEQQR NSKAAHTSKP TIHLLSPIVN
160 170 180 190 200
RDKPNNQTND RGGNDPDSPT SQRRSRGLRS LLSSGKNTIF DSISKNLDDE
210 220 230 240 250
INENAHIRND TTSSKIAGKS PSRLSALQKS PELRKERNNM ILKEHILRSK
260 270 280 290 300
DDQNITSSRK LDNIELSSIG DSTAMTSRSS TVNANDILGN EENDGITKLK
310 320 330 340
RVNKLTSSPV KRDCSTNKKR KLTKQRIATL PNSDEELSNN LNVDEFV
Length:347
Mass (Da):39,354
Last modified:November 1, 1996 - v1
Checksum:i60D880BA947B9005
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64867.1.
BK006938 Genomic DNA. Translation: DAA12276.1.
PIRiS69719.
RefSeqiNP_010727.1. NM_001180747.1.

Genome annotation databases

EnsemblFungiiYDR439W; YDR439W; YDR439W.
GeneIDi852049.
KEGGisce:YDR439W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64867.1.
BK006938 Genomic DNA. Translation: DAA12276.1.
PIRiS69719.
RefSeqiNP_010727.1. NM_001180747.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N7NX-ray3.90E/F1-102[»]
ProteinModelPortaliQ04087.
SMRiQ04087. Positions 3-33.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32495. 359 interactions.
DIPiDIP-1416N.
IntActiQ04087. 14 interactions.
MINTiMINT-391498.
STRINGi4932.YDR439W.

Proteomic databases

MaxQBiQ04087.
PaxDbiQ04087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR439W; YDR439W; YDR439W.
GeneIDi852049.
KEGGisce:YDR439W.

Organism-specific databases

CYGDiYDR439w.
SGDiS000002847. LRS4.

Phylogenomic databases

eggNOGiNOG72052.
InParanoidiQ04087.
KOiK12775.
OMAiMAHENER.
OrthoDBiEOG7673QD.

Enzyme and pathway databases

BioCyciYEAST:G3O-29973-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ04087.
NextBioi970308.

Gene expression databases

GenevestigatoriQ04087.

Family and domain databases

InterProiIPR018479. Lrs4/Mde4.
[Graphical view]
PfamiPF10422. LRS4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "A genetic screen for ribosomal DNA silencing defects identifies multiple DNA replication and chromatin-modulating factors."
    Smith J.S., Caputo E., Boeke J.D.
    Mol. Cell. Biol. 19:3184-3197(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Kinetochore recruitment of two nucleolar proteins is required for homolog segregation in meiosis I."
    Rabitsch K.P., Petronczki M., Javerzat J.-P., Genier S., Chwalla B., Schleiffer A., Tanaka T.U., Nasmyth K.
    Dev. Cell 4:535-548(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE MONOPOLIN COMPLEX.
  5. "Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae."
    Enyenihi A.H., Saunders W.S.
    Genetics 163:47-54(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Polo-like kinase Cdc5 promotes chiasmata formation and cosegregation of sister centromeres at meiosis I."
    Clyne R.K., Katis V.L., Jessop L., Benjamin K.R., Herskowitz I., Lichten M., Nasmyth K.
    Nat. Cell Biol. 5:480-485(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Spo13 maintains centromeric cohesion and kinetochore coorientation during meiosis I."
    Lee B.H., Kiburz B.M., Amon A.
    Curr. Biol. 14:2168-2182(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION TO THE KINETOCHORE.
  10. "Spo13 facilitates monopolin recruitment to kinetochores and regulates maintenance of centromeric cohesion during yeast meiosis."
    Katis V.L., Matos J., Mori S., Shirahige K., Zachariae W., Nasmyth K.
    Curr. Biol. 14:2183-2196(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  11. "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-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLRS4_YEAST
AccessioniPrimary (citable) accession number: Q04087
Secondary accession number(s): D6VT66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 99 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 1390 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.