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P25342

- CDC10_YEAST

UniProt

P25342 - CDC10_YEAST

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Protein

Cell division control protein 10

Gene

CDC10

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

Functioni

Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741GTPBy similarity
Binding sitei100 – 1001GTP; via amide nitrogenBy similarity
Binding sitei236 – 2361GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei251 – 2511GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 468GTPBy similarity
Nucleotide bindingi180 – 1889GTPBy similarity

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: SGD
  2. GTPase activity Source: SGD
  3. GTP binding Source: UniProtKB-KW
  4. protein complex scaffold Source: SGD
  5. structural molecule activity Source: SGD

GO - Biological processi

  1. exit from mitosis Source: SGD
  2. GTP catabolic process Source: GOC
  3. maintenance of cell polarity Source: SGD
  4. septin ring assembly Source: SGD
  5. sporulation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29321-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 10
Gene namesi
Name:CDC10
Ordered Locus Names:YCR002C
ORF Names:YCR022, YCR2C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCR002c.
SGDiS000000595. CDC10.

Subcellular locationi

Membrane 1 Publication; Peripheral membrane protein 1 Publication. Bud neck 1 Publication
Note: Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate.

GO - Cellular componenti

  1. ascospore-type prospore Source: SGD
  2. cellular bud neck septin ring Source: SGD
  3. mating projection base Source: SGD
  4. meiotic spindle Source: SGD
  5. prospore membrane Source: SGD
  6. septin complex Source: SGD
  7. septin filament array Source: SGD
  8. spindle microtubule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Cell division control protein 10PRO_0000173498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei216 – 2161Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP25342.
PaxDbiP25342.
PeptideAtlasiP25342.

Expressioni

Gene expression databases

GenevestigatoriP25342.

Interactioni

Subunit structurei

Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of highly ordered filaments at the mother-bud-neck. A complex formed by CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in vitro and the components seem to be present in a 2:2:2:2 arrangement in vivo. The filaments are proposed to be formed by the end-to-end polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a bridge to bundle the polymers into paired filaments. Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Self-associates. Interacts with SYP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BUD4P471362EBI-4174,EBI-3848

Protein-protein interaction databases

BioGridi30980. 187 interactions.
DIPiDIP-673N.
IntActiP25342. 13 interactions.
MINTiMINT-619481.
STRINGi4932.YCR002C.

Structurei

3D structure databases

ProteinModelPortaliP25342.
SMRiP25342. Positions 31-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 302274Septin-type GAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5019.
GeneTreeiENSGT00740000115641.
HOGENOMiHOG000233586.
InParanoidiP25342.
KOiK16938.
OMAiRKELTAM.
OrthoDBiEOG76HQBH.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25342-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPLSSVQPA SYVGFDTITN QIEHRLLKKG FQFNIMVVGQ SGLGKSTLIN
60 70 80 90 100
TLFASHLIDS ATGDDISALP VTKTTEMKIS THTLVEDRVR LNINVIDTPG
110 120 130 140 150
FGDFIDNSKA WEPIVKYIKE QHSQYLRKEL TAQRERFITD TRVHAILYFL
160 170 180 190 200
QPNGKELSRL DVEALKRLTE IANVIPVIGK SDTLTLDERT EFRELIQNEF
210 220 230 240 250
EKYNFKIYPY DSEELTDEEL ELNRSVRSII PFAVVGSENE IEINGETFRG
260 270 280 290 300
RKTRWSAINV EDINQCDFVY LREFLIRTHL QDLIETTSYI HYEGFRARQL
310 320
IALKENANSR SSAHMSSNAI QR
Length:322
Mass (Da):37,025
Last modified:May 1, 1992 - v1
Checksum:i672467301D4D2697
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16549 Genomic DNA. Translation: AAB49377.1.
S48552 Genomic DNA. Translation: AAD13856.1.
X59720 Genomic DNA. Translation: CAA42339.1.
BK006937 Genomic DNA. Translation: DAA07481.1.
PIRiS19441.
RefSeqiNP_009928.1. NM_001178715.1.

Genome annotation databases

EnsemblFungiiYCR002C; YCR002C; YCR002C.
GeneIDi850358.
KEGGisce:YCR002C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16549 Genomic DNA. Translation: AAB49377.1 .
S48552 Genomic DNA. Translation: AAD13856.1 .
X59720 Genomic DNA. Translation: CAA42339.1 .
BK006937 Genomic DNA. Translation: DAA07481.1 .
PIRi S19441.
RefSeqi NP_009928.1. NM_001178715.1.

3D structure databases

ProteinModelPortali P25342.
SMRi P25342. Positions 31-300.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 30980. 187 interactions.
DIPi DIP-673N.
IntActi P25342. 13 interactions.
MINTi MINT-619481.
STRINGi 4932.YCR002C.

Proteomic databases

MaxQBi P25342.
PaxDbi P25342.
PeptideAtlasi P25342.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YCR002C ; YCR002C ; YCR002C .
GeneIDi 850358.
KEGGi sce:YCR002C.

Organism-specific databases

CYGDi YCR002c.
SGDi S000000595. CDC10.

Phylogenomic databases

eggNOGi COG5019.
GeneTreei ENSGT00740000115641.
HOGENOMi HOG000233586.
InParanoidi P25342.
KOi K16938.
OMAi RKELTAM.
OrthoDBi EOG76HQBH.

Enzyme and pathway databases

BioCyci YEAST:G3O-29321-MONOMER.

Miscellaneous databases

NextBioi 965830.

Gene expression databases

Genevestigatori P25342.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view ]
PANTHERi PTHR18884. PTHR18884. 1 hit.
Pfami PF00735. Septin. 1 hit.
[Graphical view ]
PIRSFi PIRSF006698. Septin. 1 hit.
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51719. G_SEPTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26109 / X2180.
  2. "Sequence of the CDC10 region at chromosome III of Saccharomyces cerevisiae."
    Steensma H.Y., van der Aart Q.J.M.
    Yeast 7:425-429(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function."
    Frazier J.A., Wong M.L., Longtine M.S., Pringle J.R., Mann M., Mitchison T.J., Field C.
    J. Cell Biol. 143:737-749(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SEPTIN COMPLEX.
  6. "Cell cycle-dependent assembly of a Gin4-septin complex."
    Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.
    Mol. Biol. Cell 13:2091-2105(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE GIN4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function."
    Casamayor A., Snyder M.
    Mol. Cell. Biol. 23:2762-2777(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PHOSPHOINOSIDES LIPIDS, INTERACTION WITH CDC11.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae."
    Versele M., Gullbrand B., Shulewitz M.J., Cid V.J., Bahmanyar S., Chen R.E., Barth P., Alber T., Thorner J.
    Mol. Biol. Cell 15:4568-4583(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, ASSEMBLY OF THE SEPTIN FILAMENTS.
  11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "A novel septin-associated protein, Syp1p, is required for normal cell cycle-dependent septin cytoskeleton dynamics in yeast."
    Qiu W., Neo S.P., Yu X., Cai M.
    Genetics 180:1445-1457(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYP1.
  14. "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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDC10_YEAST
AccessioniPrimary (citable) accession number: P25342
Secondary accession number(s): D6VR12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 29, 2014
This is version 148 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 14100 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3