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P32457

- CDC3_YEAST

UniProt

P32457 - CDC3_YEAST

Protein

Cell division control protein 3

Gene

CDC3

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 141 (01 Oct 2014)
      Sequence version 3 (21 Sep 2011)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei207 – 2071GTP; via amide nitrogenBy similarity
    Binding sitei344 – 3441GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei360 – 3601GTPBy similarity
    Sitei415 – 4151Not sumoylated
    Sitei443 – 4431Not sumoylated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi126 – 1338GTPBy similarity
    Nucleotide bindingi287 – 2959GTPBy 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. septin ring assembly Source: SGD
    4. septin ring disassembly Source: SGD

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32400-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division control protein 3
    Gene namesi
    Name:CDC3
    Ordered Locus Names:YLR314C
    ORF Names:L8543.7
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR314c.
    SGDiS000004306. CDC3.

    Subcellular locationi

    Membrane; Peripheral membrane protein. Bud neck
    Note: Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate.

    GO - Cellular componenti

    1. ascospore wall Source: SGD
    2. cellular bud neck septin ring Source: SGD
    3. mating projection base Source: SGD
    4. prospore membrane Source: SGD
    5. septin complex Source: SGD
    6. septin filament array Source: SGD

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 41K → R: Abolishes sumoylation. 1 Publication
    Mutagenesisi11 – 111K → R: Abolishes sumoylation. 1 Publication
    Mutagenesisi287 – 2871K → R: Abolishes sumoylation. 1 Publication
    Mutagenesisi415 – 4151K → R: No effect on sumoylation. 1 Publication
    Mutagenesisi443 – 4431K → R: No effect on sumoylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 520519Cell division control protein 3PRO_0000173496Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei2 – 21Phosphoserine2 Publications
    Cross-linki4 – 4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei9 – 91Phosphoserine3 Publications
    Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei47 – 471Phosphothreonine2 Publications
    Modified residuei60 – 601Phosphoserine2 Publications
    Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei77 – 771Phosphoserine2 Publications
    Modified residuei175 – 1751Phosphoserine3 Publications
    Cross-linki287 – 287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei468 – 4681Phosphothreonine2 Publications
    Modified residuei509 – 5091Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by CDC28. Phosphorylation at the end of G1 may facilitate initiation of a new cell cycle by promoting disassembly of the obsolete septin ring from the previous cell cycle.5 Publications
    Sumoylated during mitosis on the mother cell side of the bud neck by UBC9/SIZ1. Sumoylation probably plays a central role in regulating septin ring disassembly during the cell cycle.4 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP32457.
    PaxDbiP32457.
    PeptideAtlasiP32457.

    Expressioni

    Gene expression databases

    GenevestigatoriP32457.

    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 SIZ1 and SYP1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GIC1P387852EBI-4429,EBI-7575
    GIC2Q066483EBI-4429,EBI-7585

    Protein-protein interaction databases

    BioGridi31579. 531 interactions.
    DIPiDIP-3010N.
    IntActiP32457. 21 interactions.
    MINTiMINT-440222.
    STRINGi4932.YLR314C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32457.
    SMRiP32457. Positions 118-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini116 – 411296Septin-type GAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili427 – 50882Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5019.
    GeneTreeiENSGT00640000091410.
    HOGENOMiHOG000233586.
    KOiK16944.
    OMAiTEKLKRM.
    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. 2 hits.
    PROSITEiPS51719. G_SEPTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P32457-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND    50
    DSERFEAAES DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV 100
    GFANLPKQWH RRSIKNGFSF NLLCVGPDGI GKTTLMKTLF NNDDIEANLV 150
    KDYEEELAND QEEEEGQGEG HENQSQEQRH KVKIKSYESV IEENGVKLNL 200
    NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI NRHSINDKRI 250
    HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK 300
    KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE 350
    NYSGNQVRGR SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL 400
    YENYRSSKLA KLGIKQDNSV FKEFDPISKQ QEEKTLHEAK LAKLEIEMKT 450
    VFQQKVSEKE KKLQKSETEL FARHKEMKEK LTKQLKALED KKKQLELSIN 500
    SASPNVNHSP VPTKKKGFLR 520
    Length:520
    Mass (Da):60,054
    Last modified:September 21, 2011 - v3
    Checksum:iDCCD4C8C16AA5E25
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti431 – 4311Q → L in AAB64515. (PubMed:9169871)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16548 Genomic DNA. Translation: AAB50034.1.
    U20618 Genomic DNA. Translation: AAB64515.1.
    BK006945 Genomic DNA. Translation: DAA09624.2.
    PIRiS53393.
    RefSeqiNP_013418.2. NM_001182203.2.

    Genome annotation databases

    EnsemblFungiiYLR314C; YLR314C; YLR314C.
    GeneIDi851024.
    KEGGisce:YLR314C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16548 Genomic DNA. Translation: AAB50034.1 .
    U20618 Genomic DNA. Translation: AAB64515.1 .
    BK006945 Genomic DNA. Translation: DAA09624.2 .
    PIRi S53393.
    RefSeqi NP_013418.2. NM_001182203.2.

    3D structure databases

    ProteinModelPortali P32457.
    SMRi P32457. Positions 118-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31579. 531 interactions.
    DIPi DIP-3010N.
    IntActi P32457. 21 interactions.
    MINTi MINT-440222.
    STRINGi 4932.YLR314C.

    Proteomic databases

    MaxQBi P32457.
    PaxDbi P32457.
    PeptideAtlasi P32457.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR314C ; YLR314C ; YLR314C .
    GeneIDi 851024.
    KEGGi sce:YLR314C.

    Organism-specific databases

    CYGDi YLR314c.
    SGDi S000004306. CDC3.

    Phylogenomic databases

    eggNOGi COG5019.
    GeneTreei ENSGT00640000091410.
    HOGENOMi HOG000233586.
    KOi K16944.
    OMAi TEKLKRM.
    OrthoDBi EOG76HQBH.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32400-MONOMER.

    Miscellaneous databases

    NextBioi 967601.
    PROi P32457.

    Gene expression databases

    Genevestigatori P32457.

    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. 2 hits.
    PROSITEi PS51719. G_SEPTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204510 / AB320.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 431.
      Strain: ATCC 204508 / S288c.
    4. "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.
    5. "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-4; LYS-11; LYS-30; LYS-63 AND LYS-287, MUTAGENESIS OF LYS-4; LYS-11; LYS-287; LYS-415 AND LYS-443, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "A novel factor required for the SUMO1/Smt3 conjugation of yeast septins."
      Takahashi Y., Toh-e A., Kikuchi Y.
      Gene 275:223-231(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH SIZ1.
    7. "Phosphorylation of the septin cdc3 in G1 by the cdc28 kinase is essential for efficient septin ring disassembly."
      Tang C.S., Reed S.I.
      Cell Cycle 1:42-49(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDC28.
    8. "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.
    9. "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: ASSOCIATION WITH PHOSPHOINOSIDES LIPIDS, INTERACTION WITH CDC11.
    10. "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.
    11. "Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses."
      Zhou W., Ryan J.J., Zhou H.
      J. Biol. Chem. 279:32262-32268(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63.
    12. "A proteomic strategy for gaining insights into protein sumoylation in yeast."
      Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., Gygi S.P.
      Mol. Cell. Proteomics 4:246-254(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63.
      Strain: EJY251-11b.
    13. "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.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    15. "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 SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-175 AND THR-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-60; SER-77; SER-175 AND SER-509, 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 nameiCDC3_YEAST
    AccessioniPrimary (citable) accession number: P32457
    Secondary accession number(s): D6VYV8, Q06161
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

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

    External Data

    Dasty 3