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P32458

- CDC11_YEAST

UniProt

P32458 - CDC11_YEAST

Protein

Cell division control protein 11

Gene

CDC11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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 nitrogenBy similarity
    Binding sitei230 – 2301GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei247 – 2471GTPBy similarity

    Regions

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

    GO - Biological processi

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

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

    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

    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.
    Mutagenesisi12 – 165RKRKH → QQQQQ: Loss of function; strongly decreases association with PI(4)P and PI(5)P.
    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 – 11Removed2 Publications
    Chaini2 – 415414Cell division control protein 11PRO_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)

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili354 – 41461Sequence AnalysisAdd
    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

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    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 139 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.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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3