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P32458 (CDC11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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 11
Gene names
Name:CDC11
Synonyms:PSL9
Ordered Locus Names:YJR076C
ORF Names:J1833
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.10

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 BEM4, KCC4, SPR28 and SYP1. Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.17

Subcellular location

Membrane. Bud neck. Note: Present at the bud neck during cell division. Interacts with phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate (PI4P and PI5P). Ref.11

Domain

The coiled coil domain is required for the interaction with CDC3 and BEM4, but not for interaction with CDC12 or with itself. Ref.10

The basic motif is essential for the association with PI4P and PI5P. Ref.10

Post-translational modification

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. Ref.7

Miscellaneous

Present with 9280 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
   DomainCoiled coil
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmaintenance of cell polarity

Inferred by curator PubMed 10882120. Source: SGD

mitotic cytokinesis

Inferred from mutant phenotype PubMed 4950437. Source: SGD

positive regulation of protein kinase activity

Inferred from direct assay PubMed 14527412. Source: SGD

   Cellular_componentascospore wall

Inferred from direct assay PubMed 8636217. Source: SGD

cellular bud neck septin ring

Inferred from direct assay PubMed 1934633. Source: SGD

cytoplasmic microtubule

Inferred from direct assay PubMed 18826657. Source: SGD

mating projection base

Inferred from direct assay Ref.1. 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.13. Source: SGD

spindle microtubule

Inferred from direct assay PubMed 18826657. Source: SGD

   Molecular_function1-phosphatidylinositol binding

Inferred from direct assay Ref.10. Source: SGD

GTP binding

Inferred from direct assay Ref.10. Source: SGD

protein binding

Inferred from physical interaction PubMed 10688190PubMed 11283351Ref.9PubMed 16371506PubMed 16429126PubMed 18467557PubMed 18719252PubMed 20489023PubMed 9813092. Source: IntAct

structural molecule activity

Inferred from direct assay PubMed 18550837. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 415414Cell division control protein 11
PRO_0000173499

Regions

Domain19 – 298280Septin-type G
Nucleotide binding29 – 368GTP By similarity
Nucleotide binding172 – 1809GTP By similarity
Coiled coil354 – 41461 Potential
Motif12 – 198Basic motif

Sites

Binding site921GTP; via amide nitrogen By similarity
Binding site2301GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2471GTP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.14 Ref.19
Modified residue21Phosphoserine Ref.14
Modified residue3051Phosphoserine Ref.15
Modified residue3271Phosphothreonine Ref.15 Ref.16
Cross-link412Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7

Experimental info

Mutagenesis12 – 165RKRKH → QQEQQ: Loss of function; abolishes association with PI(4)P and PI(5)P. Ref.10
Mutagenesis12 – 165RKRKH → QQQQQ: Loss of function; strongly decreases association with PI(4)P and PI(5)P. Ref.10
Mutagenesis291G → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
Mutagenesis321G → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
Mutagenesis341G → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
Mutagenesis351R → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
Mutagenesis401N → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius; abolishes interaction with itself. Ref.10
Mutagenesis2301G → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius. Ref.10
Mutagenesis4121K → R: Abolishes sumoylation in vitro. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P32458 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 5CFFD4CD1F6C57D4

FASTA41547,649
        10         20         30         40         50         60 
MSGIIDASSA LRKRKHLKRG ITFTVMIVGQ SGSGRSTFIN TLCGQQVVDT STTILLPTDT 

        70         80         90        100        110        120 
STEIDLQLRE ETVELEDDEG VKIQLNIIDT PGFGDSLDNS PSFEIISDYI RHQYDEILLE 

       130        140        150        160        170        180 
ESRVRRNPRF KDGRVHCCLY LINPTGHGLK EIDVEFIRQL GSLVNIIPVI SKSDSLTRDE 

       190        200        210        220        230        240 
LKLNKKLIME DIDRWNLPIY NFPFDEDEIS DEDYETNMYL RTLLPFAIIG SNEVYEMGGD 

       250        260        270        280        290        300 
VGTIRGRKYP WGILDVEDSS ISDFVILRNA LLISHLHDLK NYTHEILYER YRTEALSGES 

       310        320        330        340        350        360 
VAAESIRPNL TKLNGSSSSS TTTRRNTNPF KQSNNINNDV LNPASDMHGQ STGENNETYM 

       370        380        390        400        410 
TREEQIRLEE ERLKAFEERV QQELLLKRQE LLQREKELRE IEARLEKEAK IKQEE 

« 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: DBY939.
[2]"Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI."
Huang M.-E., Manus V., Chuat J.-C., Galibert F.
Yeast 12:869-875(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [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]"SPR28, a sixth member of the septin gene family in Saccharomyces cerevisiae that is expressed specifically in sporulating cells."
de Virgilio C., DeMarini D.J., Pringle J.R.
Microbiology 142:2897-2905(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPR28.
[6]"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.
[7]"Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins."
Johnson E.S., Blobel G.
J. Cell Biol. 147:981-994(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-412, MUTAGENESIS OF LYS-412.
[8]"Kcc4 associates with septin proteins of Saccharomyces cerevisiae."
Okuzaki D., Nojima H.
FEBS Lett. 489:197-201(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCC4.
[9]"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.
[10]"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: FUNCTION, DOMAIN, INTERACTION WITH CDC3 AND BEM4, MUTAGENESIS OF 12-ARG--HIS-16; GLY-29; GLY-32; GLY-34; ARG-35; ASN-40 AND GLY-230.
[11]"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].
[12]"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].
[13]"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.
[14]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[15]"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 SER-305 AND THR-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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.
[18]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16550 Genomic DNA. Translation: AAB50035.1.
L47993 Genomic DNA. Translation: AAB39301.1.
Z49576 Genomic DNA. Translation: CAA89604.1.
BK006943 Genomic DNA. Translation: DAA08862.1.
PIRS40911.
RefSeqNP_012610.1. NM_001181734.1.

3D structure databases

ProteinModelPortalP32458.
SMRP32458. Positions 23-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33832. 230 interactions.
DIPDIP-1656N.
IntActP32458. 26 interactions.
MINTMINT-388590.
STRING4932.YJR076C.

Proteomic databases

MaxQBP32458.
PaxDbP32458.
PeptideAtlasP32458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR076C; YJR076C; YJR076C.
GeneID853539.
KEGGsce:YJR076C.

Organism-specific databases

CYGDYJR076c.
SGDS000003837. CDC11.

Phylogenomic databases

eggNOGCOG5019.
GeneTreeENSGT00740000115641.
HOGENOMHOG000233586.
KOK16945.
OMADTSTEID.
OrthoDBEOG76HQBH.

Enzyme and pathway databases

BioCycYEAST:G3O-31706-MONOMER.

Gene expression databases

GenevestigatorP32458.

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

NextBio974251.

Entry information

Entry nameCDC11_YEAST
AccessionPrimary (citable) accession number: P32458
Secondary accession number(s): D6VWP6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 138 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 X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families