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P32458

- CDC11_YEAST

UniProt

P32458 - CDC11_YEAST

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Protein
Cell division control protein 11
Gene
CDC11, PSL9, YJR076C, J1833
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921GTP; via amide nitrogen By similarity
Binding sitei230 – 2301GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei247 – 2471GTP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 368GTP By similarity
Nucleotide bindingi172 – 1809GTP By similarity

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: SGD
  2. GTP binding Source: SGD
  3. protein binding Source: IntAct
  4. structural molecule activity Source: SGD
Complete GO annotation...

GO - Biological processi

  1. maintenance of cell polarity Source: SGD
  2. mitotic cytokinesis Source: SGD
  3. positive regulation of protein kinase activity Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-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
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR076c.
SGDiS000003837. CDC11.

Subcellular locationi

Membrane. Bud neck
Note: Present at the bud neck during cell division. Interacts with phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate (PI4P and PI5P).1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 165RKRKH → QQEQQ: Loss of function; abolishes association with PI(4)P and PI(5)P. 1 Publication
Mutagenesisi12 – 165RKRKH → QQQQQ: Loss of function; strongly decreases association with PI(4)P and PI(5)P. 1 Publication
Mutagenesisi29 – 291G → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication
Mutagenesisi32 – 321G → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication
Mutagenesisi34 – 341G → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication
Mutagenesisi35 – 351R → A: Abolishes GTP-binding; no strong effect in vivo. 1 Publication
Mutagenesisi40 – 401N → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius; abolishes interaction with itself. 1 Publication
Mutagenesisi230 – 2301G → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius. 1 Publication
Mutagenesisi412 – 4121K → R: Abolishes sumoylation in vitro. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 415414Cell division control protein 11
PRO_0000173499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei305 – 3051Phosphoserine1 Publication
Modified residuei327 – 3271Phosphothreonine2 Publications
Cross-linki412 – 412Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

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.
PeptideAtlasiP32458.

Expressioni

Gene expression databases

GenevestigatoriP32458.

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

WithEntry#Exp.IntActNotes
CDC12P324687EBI-4178,EBI-4182
GIC1P387852EBI-4178,EBI-7575
GIC2Q066482EBI-4178,EBI-7585
GIN4Q122637EBI-4178,EBI-7595
SHS1Q076575EBI-4178,EBI-22083

Protein-protein interaction databases

BioGridi33832. 230 interactions.
DIPiDIP-1656N.
IntActiP32458. 26 interactions.
MINTiMINT-388590.
STRINGi4932.YJR076C.

Structurei

3D structure databases

ProteinModelPortaliP32458.
SMRiP32458. Positions 23-298.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 298280Septin-type G
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili354 – 41461 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi12 – 198Basic motif

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

eggNOGiCOG5019.
GeneTreeiENSGT00740000115641.
HOGENOMiHOG000233586.
KOiK16945.
OMAiDTSTEID.
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.

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

P32458-1 [UniParc]FASTAAdd to Basket

« Hide

MSGIIDASSA LRKRKHLKRG ITFTVMIVGQ SGSGRSTFIN TLCGQQVVDT    50
STTILLPTDT STEIDLQLRE ETVELEDDEG VKIQLNIIDT PGFGDSLDNS 100
PSFEIISDYI RHQYDEILLE ESRVRRNPRF KDGRVHCCLY LINPTGHGLK 150
EIDVEFIRQL GSLVNIIPVI SKSDSLTRDE LKLNKKLIME DIDRWNLPIY 200
NFPFDEDEIS DEDYETNMYL RTLLPFAIIG SNEVYEMGGD VGTIRGRKYP 250
WGILDVEDSS ISDFVILRNA LLISHLHDLK NYTHEILYER YRTEALSGES 300
VAAESIRPNL TKLNGSSSSS TTTRRNTNPF KQSNNINNDV LNPASDMHGQ 350
STGENNETYM TREEQIRLEE ERLKAFEERV QQELLLKRQE LLQREKELRE 400
IEARLEKEAK IKQEE 415
Length:415
Mass (Da):47,649
Last modified:October 1, 1993 - v1
Checksum:i5CFFD4CD1F6C57D4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S40911.
RefSeqi NP_012610.1. NM_001181734.1.

3D structure databases

ProteinModelPortali P32458.
SMRi P32458. Positions 23-298.
ModBasei Search...

Protein-protein interaction databases

BioGridi 33832. 230 interactions.
DIPi DIP-1656N.
IntActi P32458. 26 interactions.
MINTi MINT-388590.
STRINGi 4932.YJR076C.

Proteomic databases

MaxQBi P32458.
PaxDbi P32458.
PeptideAtlasi P32458.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR076C ; YJR076C ; YJR076C .
GeneIDi 853539.
KEGGi sce:YJR076C.

Organism-specific databases

CYGDi YJR076c.
SGDi S000003837. CDC11.

Phylogenomic databases

eggNOGi COG5019.
GeneTreei ENSGT00740000115641.
HOGENOMi HOG000233586.
KOi K16945.
OMAi DTSTEID.
OrthoDBi EOG76HQBH.

Enzyme and pathway databases

BioCyci YEAST:G3O-31706-MONOMER.

Miscellaneous databases

NextBioi 974251.

Gene expression databases

Genevestigatori P32458.

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: 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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDC11_YEAST
AccessioniPrimary (citable) accession number: P32458
Secondary accession number(s): D6VWP6
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3

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