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P32457

- CDC3_YEAST

UniProt

P32457 - CDC3_YEAST

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
InParanoidiP32457.
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

        10         20         30         40         50
MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND
60 70 80 90 100
DSERFEAAES DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV
110 120 130 140 150
GFANLPKQWH RRSIKNGFSF NLLCVGPDGI GKTTLMKTLF NNDDIEANLV
160 170 180 190 200
KDYEEELAND QEEEEGQGEG HENQSQEQRH KVKIKSYESV IEENGVKLNL
210 220 230 240 250
NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI NRHSINDKRI
260 270 280 290 300
HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK
310 320 330 340 350
KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE
360 370 380 390 400
NYSGNQVRGR SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL
410 420 430 440 450
YENYRSSKLA KLGIKQDNSV FKEFDPISKQ QEEKTLHEAK LAKLEIEMKT
460 470 480 490 500
VFQQKVSEKE KKLQKSETEL FARHKEMKEK LTKQLKALED KKKQLELSIN
510 520
SASPNVNHSP VPTKKKGFLR
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 ENSGT00760000118899.
HOGENOMi HOG000233586.
InParanoidi P32457.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 142 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