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Protein

Cell division control protein 11

Gene

CDC11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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.1 Publication

Miscellaneous

Present with 9280 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei92GTP; via amide nitrogenBy similarity1
Binding sitei230GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei247GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 36GTPBy similarity8
Nucleotide bindingi172 – 180GTPBy similarity9

GO - Molecular functioni

  • GTP binding Source: SGD
  • identical protein binding Source: IntAct
  • phosphatidylinositol-4-phosphate binding Source: SGD
  • phosphatidylinositol-5-phosphate binding Source: SGD
  • structural molecule activity Source: SGD

GO - Biological processi

  • maintenance of cell polarity Source: SGD
  • mitotic cytokinesis Source: SGD
  • positive regulation of protein kinase activity Source: SGD
  • protein localization to bud neck Source: SGD

Keywordsi

Biological processCell cycle, Cell division
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31706-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 11
Gene namesi
Name:CDC11
Synonyms:PSL9
Ordered Locus Names:YJR076C
ORF Names:J1833
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR076C
SGDiS000003837 CDC11

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12 – 16RKRKH → QQEQQ: Loss of function; abolishes association with PI(4)P and PI(5)P. 1 Publication5
Mutagenesisi12 – 16RKRKH → QQQQQ: Loss of function; strongly decreases association with PI(4)P and PI(5)P. 1 Publication5
Mutagenesisi29G → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication1
Mutagenesisi32G → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication1
Mutagenesisi34G → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication1
Mutagenesisi35R → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication1
Mutagenesisi40N → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius; abolishes interaction with itself. 1 Publication1
Mutagenesisi230G → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius. 1 Publication1
Mutagenesisi412K → R: Abolishes sumoylation in vitro. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001734992 – 415Cell division control protein 11Add BLAST414

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei305PhosphoserineCombined sources1
Modified residuei327PhosphothreonineCombined sources1
Cross-linki412Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Sumoylated during mitosis on the mother cell side of the bud neck. Sumoylation probably plays a central role in regulating septin ring disassembly during the cell cycle.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32458
PaxDbiP32458
PRIDEiP32458

PTM databases

iPTMnetiP32458

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 BEM4, KCC4, SPR28 and SYP1.6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi33832, 1212 interactors
DIPiDIP-1656N
ELMiP32458
IntActiP32458, 51 interactors
MINTiP32458
STRINGi4932.YJR076C

Structurei

Secondary structure

1415
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 29Combined sources7
Beta strandi31 – 33Combined sources3
Turni36 – 40Combined sources5
Beta strandi69 – 73Combined sources5
Beta strandi79 – 81Combined sources3
Beta strandi85 – 89Combined sources5
Helixi104 – 120Combined sources17
Beta strandi137 – 142Combined sources6
Beta strandi145 – 148Combined sources4
Helixi151 – 160Combined sources10
Turni161 – 163Combined sources3
Beta strandi166 – 172Combined sources7
Helixi173 – 175Combined sources3
Helixi178 – 194Combined sources17
Beta strandi206 – 209Combined sources4
Helixi213 – 223Combined sources11
Beta strandi230 – 232Combined sources3
Beta strandi263 – 265Combined sources3
Helixi269 – 285Combined sources17
Helixi287 – 295Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AR1X-ray2.85A20-298[»]
ProteinModelPortaliP32458
SMRiP32458
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 298Septin-type GAdd BLAST280

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili354 – 414Sequence analysisAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi12 – 19Basic motif8

Domaini

The coiled coil domain is required for the interaction with CDC3 and BEM4, but not for interaction with CDC12 or with itself.1 Publication
The basic motif is essential for the association with PI4P and PI5P.1 Publication

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00880000138554
HOGENOMiHOG000233586
InParanoidiP32458
KOiK16945
OMAiRSRQYPW
OrthoDBiEOG092C3HL6

Family and domain databases

CDDicd01850 CDC_Septin, 1 hit
InterProiView protein in InterPro
IPR030379 G_SEPTIN_dom
IPR027417 P-loop_NTPase
IPR016491 Septin
PfamiView protein in Pfam
PF00735 Septin, 1 hit
PIRSFiPIRSF006698 Septin, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51719 G_SEPTIN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGIIDASSA LRKRKHLKRG ITFTVMIVGQ SGSGRSTFIN TLCGQQVVDT
60 70 80 90 100
STTILLPTDT STEIDLQLRE ETVELEDDEG VKIQLNIIDT PGFGDSLDNS
110 120 130 140 150
PSFEIISDYI RHQYDEILLE ESRVRRNPRF KDGRVHCCLY LINPTGHGLK
160 170 180 190 200
EIDVEFIRQL GSLVNIIPVI SKSDSLTRDE LKLNKKLIME DIDRWNLPIY
210 220 230 240 250
NFPFDEDEIS DEDYETNMYL RTLLPFAIIG SNEVYEMGGD VGTIRGRKYP
260 270 280 290 300
WGILDVEDSS ISDFVILRNA LLISHLHDLK NYTHEILYER YRTEALSGES
310 320 330 340 350
VAAESIRPNL TKLNGSSSSS TTTRRNTNPF KQSNNINNDV LNPASDMHGQ
360 370 380 390 400
STGENNETYM TREEQIRLEE ERLKAFEERV QQELLLKRQE LLQREKELRE
410
IEARLEKEAK IKQEE
Length:415
Mass (Da):47,649
Last modified:October 1, 1993 - v1
Checksum:i5CFFD4CD1F6C57D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16550 Genomic DNA Translation: AAB50035.1
L47993 Genomic DNA Translation: AAB39301.1
Z49576 Genomic DNA Translation: CAA89604.1
BK006943 Genomic DNA Translation: DAA08862.1
PIRiS40911
RefSeqiNP_012610.1, NM_001181734.1

Genome annotation databases

EnsemblFungiiYJR076C; YJR076C; YJR076C
GeneIDi853539
KEGGisce:YJR076C

Similar proteinsi

Entry informationi

Entry nameiCDC11_YEAST
AccessioniPrimary (citable) accession number: P32458
Secondary accession number(s): D6VWP6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 28, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health