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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: 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)DescriptionActionsGraphical viewLength
Binding sitei74GTPBy similarity1
Binding sitei100GTP; via amide nitrogenBy similarity1
Binding sitei236GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei251GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi39 – 46GTPBy similarity8
Nucleotide bindingi180 – 188GTPBy similarity9

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: SGD
  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB-KW
  • phosphatidylinositol-4-phosphate binding Source: SGD
  • phosphatidylinositol-5-phosphate binding Source: SGD
  • protein complex scaffold Source: SGD
  • structural molecule activity Source: SGD

GO - Biological processi

  • exit from mitosis Source: SGD
  • maintenance of cell polarity Source: SGD
  • mitotic cytokinesis Source: SGD
  • septin ring assembly Source: SGD
  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR002C.
SGDiS000000595. CDC10.

Subcellular locationi

GO - Cellular componenti

  • ascospore-type prospore Source: SGD
  • cellular bud neck septin ring Source: SGD
  • mating projection base Source: SGD
  • meiotic spindle Source: SGD
  • prospore membrane Source: SGD
  • septin complex Source: SGD
  • septin filament array Source: SGD
  • spindle microtubule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001734981 – 322Cell division control protein 10Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei216PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP25342.
PRIDEiP25342.

PTM databases

iPTMnetiP25342.

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

GO - Molecular functioni

  • protein complex scaffold Source: SGD

Protein-protein interaction databases

BioGridi30980. 195 interactors.
DIPiDIP-673N.
IntActiP25342. 13 interactors.
MINTiMINT-619481.

Structurei

3D structure databases

ProteinModelPortaliP25342.
SMRiP25342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 302Septin-type GAdd BLAST274

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00860000133688.
HOGENOMiHOG000233586.
InParanoidiP25342.
KOiK16938.
OMAiDEGKNHE.
OrthoDBiEOG092C3HL6.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
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

EnsemblFungiiCAA42339; CAA42339; CAA42339.
YCR002C; 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.
PIRiS19441.
RefSeqiNP_009928.1. NM_001178715.1.

3D structure databases

ProteinModelPortaliP25342.
SMRiP25342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30980. 195 interactors.
DIPiDIP-673N.
IntActiP25342. 13 interactors.
MINTiMINT-619481.

PTM databases

iPTMnetiP25342.

Proteomic databases

MaxQBiP25342.
PRIDEiP25342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42339; CAA42339; CAA42339.
YCR002C; YCR002C; YCR002C.
GeneIDi850358.
KEGGisce:YCR002C.

Organism-specific databases

EuPathDBiFungiDB:YCR002C.
SGDiS000000595. CDC10.

Phylogenomic databases

GeneTreeiENSGT00860000133688.
HOGENOMiHOG000233586.
InParanoidiP25342.
KOiK16938.
OMAiDEGKNHE.
OrthoDBiEOG092C3HL6.

Enzyme and pathway databases

BioCyciYEAST:G3O-29321-MONOMER.

Miscellaneous databases

PROiP25342.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 169 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

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 one 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.