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P32457 (CDC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. 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 3
Gene names
Name:CDC3
Ordered Locus Names:YLR314C
ORF Names:L8543.7
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length520 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.

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 SIZ1 and SYP1. Ref.4 Ref.6 Ref.8 Ref.9 Ref.16

Subcellular location

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.

Post-translational modification

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. Ref.7

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. Ref.5 Ref.6

Sequence similarities

Belongs to the septin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GIC1P387852EBI-4429,EBI-7575
GIC2Q066483EBI-4429,EBI-7585

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 520519Cell division control protein 3
PRO_0000173496

Regions

Nucleotide binding126 – 1338GTP By similarity
Nucleotide binding287 – 2959GTP By similarity
Coiled coil427 – 50882 Potential

Sites

Binding site2071GTP; via amide nitrogen By similarity
Binding site3441GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site3601GTP By similarity
Site4151Not sumoylated
Site4431Not sumoylated

Amino acid modifications

Modified residue21N-acetylserine Ref.13 Ref.19
Modified residue21Phosphoserine Ref.13
Modified residue91Phosphoserine Ref.15 Ref.17
Modified residue471Phosphothreonine Ref.18
Modified residue601Phosphoserine Ref.18
Modified residue771Phosphoserine Ref.18
Modified residue1751Phosphoserine Ref.17 Ref.18
Modified residue4681Phosphothreonine Ref.17
Modified residue5091Phosphoserine Ref.18
Cross-link4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5
Cross-link30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5 Ref.11 Ref.12
Cross-link287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.5

Experimental info

Mutagenesis41K → R: Abolishes sumoylation. Ref.5
Mutagenesis111K → R: Abolishes sumoylation. Ref.5
Mutagenesis2871K → R: Abolishes sumoylation. Ref.5
Mutagenesis4151K → R: No effect on sumoylation. Ref.5
Mutagenesis4431K → R: No effect on sumoylation. Ref.5
Sequence conflict4311Q → L in AAB64515. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32457 [UniParc].

Last modified September 21, 2011. Version 3.
Checksum: DCCD4C8C16AA5E25

FASTA52060,054
        10         20         30         40         50         60 
MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND DSERFEAAES 

        70         80         90        100        110        120 
DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV GFANLPKQWH RRSIKNGFSF 

       130        140        150        160        170        180 
NLLCVGPDGI GKTTLMKTLF NNDDIEANLV KDYEEELAND QEEEEGQGEG HENQSQEQRH 

       190        200        210        220        230        240 
KVKIKSYESV IEENGVKLNL NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI 

       250        260        270        280        290        300 
NRHSINDKRI HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK 

       310        320        330        340        350        360 
KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE NYSGNQVRGR 

       370        380        390        400        410        420 
SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL YENYRSSKLA KLGIKQDNSV 

       430        440        450        460        470        480 
FKEFDPISKQ QEEKTLHEAK LAKLEIEMKT VFQQKVSEKE KKLQKSETEL FARHKEMKEK 

       490        500        510        520 
LTKQLKALED KKKQLELSIN SASPNVNHSP VPTKKKGFLR 

« 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: 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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
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]"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
L16548 Genomic DNA. Translation: AAB50034.1.
U20618 Genomic DNA. Translation: AAB64515.1.
BK006945 Genomic DNA. Translation: DAA09624.2.
PIRS53393.
RefSeqNP_013418.2. NM_001182203.2.

3D structure databases

ProteinModelPortalP32457.
SMRP32457. Positions 118-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31579. 531 interactions.
DIPDIP-3010N.
IntActP32457. 21 interactions.
MINTMINT-440222.
STRING4932.YLR314C.

Proteomic databases

PaxDbP32457.
PeptideAtlasP32457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR314C; YLR314C; YLR314C.
GeneID851024.
KEGGsce:YLR314C.

Organism-specific databases

CYGDYLR314c.
SGDS000004306. CDC3.

Phylogenomic databases

eggNOGCOG5019.
GeneTreeENSGT00640000091410.
HOGENOMHOG000233586.
KOK16944.
OMAQNDDSER.
OrthoDBEOG76HQBH.

Enzyme and pathway databases

BioCycYEAST:G3O-32400-MONOMER.

Gene expression databases

GenevestigatorP32457.

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. 2 hits.
ProtoNetSearch...

Other

NextBio967601.
PROP32457.

Entry information

Entry nameCDC3_YEAST
AccessionPrimary (citable) accession number: P32457
Secondary accession number(s): D6VYV8, Q06161
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families