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Protein

Monopolin complex subunit CSM1

Gene

CSM1

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. Plays also a mitotic role in DNA replication.5 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • homologous chromosome segregation Source: SGD
  • meiotic chromosome segregation Source: SGD
  • protein localization to nucleolar rDNA repeats Source: SGD
  • rDNA condensation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Meiosis

Enzyme and pathway databases

BioCyciYEAST:G3O-29381-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Monopolin complex subunit CSM1
Alternative name(s):
Chromosome segregation in meiosis protein 1
Gene namesi
Name:CSM1
Synonyms:SPO86
Ordered Locus Names:YCR086W
ORF Names:YCR86W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome III

Organism-specific databases

CYGDiYCR086w.
EuPathDBiFungiDB:YCR086W.
SGDiS000000682. CSM1.

Subcellular locationi

GO - Cellular componenti

  • monopolin complex Source: SGD
  • nuclear envelope Source: SGD
  • nucleolus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Monopolin complex subunit CSM1PRO_0000202577Add
BLAST

Proteomic databases

MaxQBiP25651.
PaxDbiP25651.
PeptideAtlasiP25651.

Interactioni

Subunit structurei

Component of the monopolin complex composed of at least CSM1, LRS4 and MAM1. The complex associates with the kinetochore. Interacts with CDC46, CDC47, GIC1, GIC2, MCM3 and NUR1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-22001,EBI-22001
DSE3Q087293EBI-22001,EBI-32325
DSN1P405683EBI-22001,EBI-25398
LRS4Q0408716EBI-22001,EBI-32189
MAM1P400658EBI-22001,EBI-22643
MCM3P242792EBI-22001,EBI-10541
MCM5P294962EBI-22001,EBI-10549
MCM7P381323EBI-22001,EBI-4300
TOF2Q022084EBI-22001,EBI-27048

Protein-protein interaction databases

BioGridi31058. 281 interactions.
DIPiDIP-1283N.
IntActiP25651. 54 interactions.
MINTiMINT-391333.
STRINGi4932.YCR086W.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 155Combined sources
Helixi71 – 8212Combined sources
Beta strandi83 – 919Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi116 – 1227Combined sources
Turni126 – 1283Combined sources
Beta strandi131 – 1377Combined sources
Beta strandi139 – 1413Combined sources
Helixi143 – 1508Combined sources
Helixi155 – 1584Combined sources
Beta strandi161 – 1644Combined sources
Helixi165 – 1673Combined sources
Helixi168 – 17912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N4RX-ray2.60A/B/C/D69-181[»]
3N4SX-ray2.35A/B/C/D69-181[»]
3N4XX-ray3.41A/B/C/D1-190[»]
3N7NX-ray3.90A/B/C/D1-190[»]
4EMCX-ray3.05A/B1-190[»]
ProteinModelPortaliP25651.
SMRiP25651. Positions 13-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25651.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili31 – 7040Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG43170.
HOGENOMiHOG000000914.
InParanoidiP25651.
OMAiMDYKLGF.
OrthoDBiEOG7S4XJP.

Family and domain databases

InterProiIPR020981. Monopolin_cplx_su-Csm1/Pcs1.
[Graphical view]
PfamiPF12539. Csm1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPLTVYKNS VKQQIDSADL LVANLVNENF VLSEKLDTKA TEIKQLQKQI
60 70 80 90 100
DSLNAQVKEL KTQTSQQAEN SEVIKDLYEY LCNVRVHKSY EDDSGLWFDI
110 120 130 140 150
SQGTHSGGSS DDYSIMDYKL GFVKGQAQVT EVIYAPVLKQ RSTEELYSLQ
160 170 180 190
SKLPEYLFET LSFPLSSLNQ FYNKIAKSLN KKREKKDETE
Length:190
Mass (Da):21,751
Last modified:May 1, 1992 - v1
Checksum:i9650E0DA89B31CC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42261.1.
AY558153 Genomic DNA. Translation: AAS56479.1.
BK006937 Genomic DNA. Translation: DAA07555.1.
PIRiS19501.
RefSeqiNP_010009.1. NM_001178792.1.

Genome annotation databases

EnsemblFungiiYCR086W; YCR086W; YCR086W.
GeneIDi850447.
KEGGisce:YCR086W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42261.1.
AY558153 Genomic DNA. Translation: AAS56479.1.
BK006937 Genomic DNA. Translation: DAA07555.1.
PIRiS19501.
RefSeqiNP_010009.1. NM_001178792.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N4RX-ray2.60A/B/C/D69-181[»]
3N4SX-ray2.35A/B/C/D69-181[»]
3N4XX-ray3.41A/B/C/D1-190[»]
3N7NX-ray3.90A/B/C/D1-190[»]
4EMCX-ray3.05A/B1-190[»]
ProteinModelPortaliP25651.
SMRiP25651. Positions 13-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31058. 281 interactions.
DIPiDIP-1283N.
IntActiP25651. 54 interactions.
MINTiMINT-391333.
STRINGi4932.YCR086W.

Proteomic databases

MaxQBiP25651.
PaxDbiP25651.
PeptideAtlasiP25651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCR086W; YCR086W; YCR086W.
GeneIDi850447.
KEGGisce:YCR086W.

Organism-specific databases

CYGDiYCR086w.
EuPathDBiFungiDB:YCR086W.
SGDiS000000682. CSM1.

Phylogenomic databases

eggNOGiNOG43170.
HOGENOMiHOG000000914.
InParanoidiP25651.
OMAiMDYKLGF.
OrthoDBiEOG7S4XJP.

Enzyme and pathway databases

BioCyciYEAST:G3O-29381-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25651.
NextBioi966060.
PROiP25651.

Family and domain databases

InterProiIPR020981. Monopolin_cplx_su-Csm1/Pcs1.
[Graphical view]
PfamiPF12539. Csm1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: FUNCTION.
  5. Cited for: INTERACTION WITH GIC1 AND GIC2, SUBCELLULAR LOCATION.
  6. "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.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Saccharomyces cerevisiae CSM1 gene encoding a protein influencing chromosome segregation in meiosis I interacts with elements of the DNA replication complex."
    Wysocka M., Rytka J., Kurlandzka A.
    Exp. Cell Res. 294:592-602(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC46; CDC47 AND MCM3.
  10. "A DNA integrity network in the yeast Saccharomyces cerevisiae."
    Pan X., Ye P., Yuan D.S., Wang X., Bader J.S., Boeke J.D.
    Cell 124:1069-1081(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Role for perinuclear chromosome tethering in maintenance of genome stability."
    Mekhail K., Seebacher J., Gygi S.P., Moazed D.
    Nature 456:667-670(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUR1.

Entry informationi

Entry nameiCSM1_YEAST
AccessioniPrimary (citable) accession number: P25651
Secondary accession number(s): D6VR86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 122 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 1920 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.