P32458 (CDC11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division control protein 11

Gene names

Name:	CDC11
Synonyms:	PSL9
Ordered Locus Names:	YJR076C
ORF Names:	J1833

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.10
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 BEM4, KCC4, SPR28 and SYP1. Ref.4 Ref.5 Ref.7 Ref.8 Ref.10 Ref.17
Subcellular location	Membrane. Bud neck. Note: Present at the bud neck during cell division. Interacts with phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate (PI4P and PI5P). Ref.11
Domain	The coiled coil domain is required for the interaction with CDC3 and BEM4, but not for interaction with CDC12 or with itself. Ref.10 The basic motif is essential for the association with PI4P and PI5P. Ref.10
Post-translational modification	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. Ref.6
Miscellaneous	Present with 9280 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the septin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Membrane
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle cytokinesis Inferred from mutant phenotype PubMed 4950437. Source: SGD maintenance of cell polarity Inferred by curator PubMed 10882120. Source: SGD positive regulation of protein kinase activity Inferred from direct assay PubMed 14527412. Source: SGD
Cellular_component	ascospore wall Inferred from direct assay PubMed 8636217. Source: SGD cellular bud neck septin ring Inferred from direct assay PubMed 1934633. Source: SGD cytoplasmic microtubule Inferred from direct assay PubMed 18826657. Source: SGD mating projection base Inferred from direct assay PubMed 8791410. Source: SGD mating projection tip Inferred from direct assay PubMed 19053807. Source: SGD meiotic spindle Inferred from direct assay PubMed 18826657. Source: SGD prospore membrane Inferred from direct assay PubMed 18826657. Source: SGD septin complex Inferred from direct assay PubMed 18550837. Source: SGD septin filament array Inferred from direct assay Ref.13. Source: SGD spindle microtubule Inferred from direct assay PubMed 18826657. Source: SGD
Molecular_function	1-phosphatidylinositol binding Inferred from direct assay Ref.10. Source: SGD GTP binding Inferred from direct assay Ref.10. Source: SGD structural molecule activity Inferred from direct assay PubMed 18550837. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC10	P25342	9	EBI-4178,EBI-4174
CDC12	P32468	10	EBI-4178,EBI-4182
GIC1	P38785	2	EBI-4178,EBI-7575
GIC2	Q06648	2	EBI-4178,EBI-7585
GIN4	Q12263	7	EBI-4178,EBI-7595
SHS1	Q07657	5	EBI-4178,EBI-22083

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 415	415	Cell division control protein 11		PRO_0000173499
Regions
	Nucleotide binding	29 – 36	8	GTP By similarity
	Nucleotide binding	172 – 180	9	GTP By similarity
	Coiled coil	354 – 414	61	Potential
	Motif	12 – 19	8	Basic motif
Sites
	Binding site	92	1	GTP; via amide nitrogen By similarity
	Binding site	230	1	GTP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	247	1	GTP By similarity
Amino acid modifications
	Modified residue	305	1	Phosphoserine Ref.14
	Modified residue	316	1	Phosphoserine Ref.9 Ref.16 Ref.18
	Modified residue	317	1	Phosphoserine Ref.18
	Modified residue	318	1	Phosphoserine Ref.16
	Modified residue	319	1	Phosphoserine Ref.9 Ref.16 Ref.18
	Modified residue	320	1	Phosphoserine Ref.16
	Modified residue	327	1	Phosphothreonine Ref.14 Ref.15 Ref.16
	Cross-link	412		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6
Experimental info
	Mutagenesis	12 – 16	5	RKRKH → QQEQQ: Loss of function; abolishes association with PI(4)P and PI(5)P. Ref.10
	Mutagenesis	12 – 16	5	RKRKH → QQQQQ: Loss of function; strongly decreases association with PI(4)P and PI(5)P. Ref.10
	Mutagenesis	29	1	G → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
	Mutagenesis	32	1	G → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
	Mutagenesis	34	1	G → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
	Mutagenesis	35	1	R → A: Abolishes GTP-binding; no strong effect in vivo. Ref.10
	Mutagenesis	40	1	N → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius; abolishes interaction with itself. Ref.10
	Mutagenesis	230	1	G → E: Temperature-sensitive; no effect at 23 degrees Celsius but loss of function at 37 degrees Celsius. Ref.10
	Mutagenesis	412	1	K → R: Abolishes sumoylation in vitro. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P32458 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 5CFFD4CD1F6C57D4	FASTA	415	47,649
	10 20 30 40 50 60 MSGIIDASSA LRKRKHLKRG ITFTVMIVGQ SGSGRSTFIN TLCGQQVVDT STTILLPTDT 70 80 90 100 110 120 STEIDLQLRE ETVELEDDEG VKIQLNIIDT PGFGDSLDNS PSFEIISDYI RHQYDEILLE 130 140 150 160 170 180 ESRVRRNPRF KDGRVHCCLY LINPTGHGLK EIDVEFIRQL GSLVNIIPVI SKSDSLTRDE 190 200 210 220 230 240 LKLNKKLIME DIDRWNLPIY NFPFDEDEIS DEDYETNMYL RTLLPFAIIG SNEVYEMGGD 250 260 270 280 290 300 VGTIRGRKYP WGILDVEDSS ISDFVILRNA LLISHLHDLK NYTHEILYER YRTEALSGES 310 320 330 340 350 360 VAAESIRPNL TKLNGSSSSS TTTRRNTNPF KQSNNINNDV LNPASDMHGQ STGENNETYM 370 380 390 400 410 TREEQIRLEE ERLKAFEERV QQELLLKRQE LLQREKELRE IEARLEKEAK IKQEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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: DBY939.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[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: MASS SPECTROMETRY, IDENTIFICATION IN THE GIN4 COMPLEX.
[9]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-319, MASS SPECTROMETRY. Strain: 2124.
[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]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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]	"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, MASS SPECTROMETRY. 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 THR-327, MASS SPECTROMETRY.
[16]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-318; SER-319; SER-320 AND THR-327, MASS SPECTROMETRY.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-317 AND SER-319, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L16550 Genomic DNA. Translation: AAB50035.1. Z49576 Genomic DNA. Translation: CAA89604.1. L47993 Genomic DNA. Translation: AAB39301.1. BK006943 Genomic DNA. Translation: DAA08862.1.
PIR	S40911.
RefSeq	NP_012610.1. NM_001181734.1.
3D structure databases
ProteinModelPortal	P32458.
SMR	P32458. Positions 23-298.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1656N.
IntAct	P32458. 33 interactions.
MINT	MINT-388590.
STRING	4932.YJR076C.
Proteomic databases
PaxDb	P32458.
PeptideAtlas	P32458.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJR076C; YJR076C; YJR076C.
GeneID	853539.
KEGG	sce:YJR076C.
Organism-specific databases
CYGD	YJR076c.
SGD	S000003837. CDC11.
Phylogenomic databases
eggNOG	COG5019.
GeneTree	ENSGT00550000075461.
HOGENOM	HOG000233586.
OrthoDB	EOG4CJZRV.
Gene expression databases
Genevestigator	P32458.
GermOnline	YJR076C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000038. Cell_div_GTP-bd. IPR016491. Septin. [Graphical view]
PANTHER	PTHR18884. PTHR18884. 1 hit.
Pfam	PF00735. Septin. 1 hit. [Graphical view]
PIRSF	PIRSF006698. Septin. 1 hit.
ProtoNet	Search...
Other
NextBio	974251.

Entry information

Entry name

CDC11_YEAST

Accession

Primary (citable) accession number: P32458
Secondary accession number(s): D6VWP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program