Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25342 (CDC10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division control protein 10
Gene names
Name:CDC10
Ordered Locus Names:YCR002C
ORF Names:YCR022, YCR2C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.13

Subcellular location

Membrane; Peripheral membrane protein. Bud neck. Note: Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate. Ref.8

Miscellaneous

Present with 14100 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.

Contains 1 septin-type G (guanine nucleotide-binding) domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentMembrane
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay PubMed 14993234. Source: GOC

exit from mitosis

Inferred from mutant phenotype PubMed 12699621. Source: SGD

maintenance of cell polarity

Inferred by curator PubMed 10882120. Source: SGD

septin ring assembly

Inferred from mutant phenotype PubMed 14993234. Source: SGD

sporulation

Inferred from direct assay PubMed 18701287. Source: SGD

   Cellular_componentascospore-type prospore

Inferred from direct assay PubMed 18701287. Source: SGD

cellular bud neck septin ring

Inferred from direct assay PubMed 9884239. Source: SGD

mating projection base

Inferred from direct assay PubMed 18552279. Source: SGD

meiotic spindle

Inferred from direct assay PubMed 18826657. Source: SGD

prospore membrane

Inferred from direct assay PubMed 18826657. Source: SGD

septin complex

Inferred from direct assay PubMed 18550837. Source: SGD

septin filament array

Inferred from direct assay Ref.10. Source: SGD

spindle microtubule

Inferred from direct assay PubMed 18826657. Source: SGD

   Molecular_function1-phosphatidylinositol binding

Inferred from direct assay Ref.7. Source: SGD

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay PubMed 14993234. Source: SGD

protein binding

Inferred from physical interaction PubMed 16429126PubMed 20489023. Source: IntAct

protein complex scaffold

Inferred from direct assay PubMed 15901837. Source: SGD

structural molecule activity

Inferred from direct assay PubMed 18550837. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BUD4P471362EBI-4174,EBI-3848

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Cell division control protein 10
PRO_0000173498

Regions

Domain29 – 302274Septin-type G
Nucleotide binding39 – 468GTP By similarity
Nucleotide binding180 – 1889GTP By similarity

Sites

Binding site741GTP By similarity
Binding site1001GTP; via amide nitrogen By similarity
Binding site2361GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2511GTP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue2161Phosphothreonine Ref.11 Ref.14

Sequences

Sequence LengthMass (Da)Tools
P25342 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 672467301D4D2697

FASTA32237,025
        10         20         30         40         50         60 
MDPLSSVQPA SYVGFDTITN QIEHRLLKKG FQFNIMVVGQ SGLGKSTLIN TLFASHLIDS 

        70         80         90        100        110        120 
ATGDDISALP VTKTTEMKIS THTLVEDRVR LNINVIDTPG FGDFIDNSKA WEPIVKYIKE 

       130        140        150        160        170        180 
QHSQYLRKEL TAQRERFITD TRVHAILYFL QPNGKELSRL DVEALKRLTE IANVIPVIGK 

       190        200        210        220        230        240 
SDTLTLDERT EFRELIQNEF EKYNFKIYPY DSEELTDEEL ELNRSVRSII PFAVVGSENE 

       250        260        270        280        290        300 
IEINGETFRG RKTRWSAINV EDINQCDFVY LREFLIRTHL QDLIETTSYI HYEGFRARQL 

       310        320 
IALKENANSR SSAHMSSNAI QR 

« Hide

References

« Hide 'large scale' references
[1]"The septins: roles in cytokinesis and other processes."
Longtine M.S., DeMarini D.J., Valencik M.L., Al-Awar O.S., Fares H., De Virgilio C., Pringle J.R.
Curr. Opin. Cell Biol. 8:106-119(1996) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"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].
[9]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16549 Genomic DNA. Translation: AAB49377.1.
S48552 Genomic DNA. Translation: AAD13856.1.
X59720 Genomic DNA. Translation: CAA42339.1.
BK006937 Genomic DNA. Translation: DAA07481.1.
PIRS19441.
RefSeqNP_009928.1. NM_001178715.1.

3D structure databases

ProteinModelPortalP25342.
SMRP25342. Positions 31-300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30980. 186 interactions.
DIPDIP-673N.
IntActP25342. 13 interactions.
MINTMINT-619481.
STRING4932.YCR002C.

Proteomic databases

MaxQBP25342.
PaxDbP25342.
PeptideAtlasP25342.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR002C; YCR002C; YCR002C.
GeneID850358.
KEGGsce:YCR002C.

Organism-specific databases

CYGDYCR002c.
SGDS000000595. CDC10.

Phylogenomic databases

eggNOGCOG5019.
GeneTreeENSGT00740000115641.
HOGENOMHOG000233586.
KOK16938.
OMARKELTAM.
OrthoDBEOG76HQBH.

Enzyme and pathway databases

BioCycYEAST:G3O-29321-MONOMER.

Gene expression databases

GenevestigatorP25342.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965830.

Entry information

Entry nameCDC10_YEAST
AccessionPrimary (citable) accession number: P25342
Secondary accession number(s): D6VR12
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families