P25342 (CDC10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division control protein 10

Gene names

Name:	CDC10
Ordered Locus Names:	YCR002C
ORF Names:	YCR2C, YCR022

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	322 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 assymetrically 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.
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. Ref.8
Miscellaneous	Present with 14100 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the septin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle cytokinesis Inferred from direct assay. Source: SGD exit from mitosis Inferred from mutant phenotype. Source: SGD maintenance of cell polarity Inferred by curator. Source: SGD septin ring assembly Inferred from mutant phenotype. Source: SGD sporulation Inferred from direct assay. Source: SGD
Cellular component	cellular bud neck septin ring Inferred from direct assay. Source: SGD mating projection base Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD meiotic spindle Inferred from direct assay. Source: SGD prospore membrane Inferred from direct assay. Source: SGD septin complex Inferred from direct assay. Source: SGD septin filament array Inferred from direct assay Ref.10. Source: SGD spindle microtubule Inferred from direct assay. Source: SGD
Molecular function	1-phosphatidylinositol binding Inferred from direct assay Ref.7. Source: SGD GTP binding Inferred from direct assay. Source: SGD GTPase activity Inferred from direct assay. Source: SGD protein complex scaffold Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD4	P47136	2	EBI-4174,EBI-3848
CDC11	P32458	9	EBI-4174,EBI-4178

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 322	322	Cell division control protein 10		PRO_0000173498
Regions
	Nucleotide binding	39 – 46	8	GTP By similarity
	Nucleotide binding	180 – 188	9	GTP By similarity
Sites
	Binding site	74	1	GTP By similarity
	Binding site	100	1	GTP; via amide nitrogen By similarity
	Binding site	236	1	GTP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	251	1	GTP By similarity
Amino acid modifications
	Modified residue	67	1	Phosphoserine Ref.14
	Modified residue	216	1	Phosphothreonine Ref.11 Ref.14
	Modified residue	311	1	Phosphoserine Ref.14
	Modified residue	312	1	Phosphoserine Ref.13 Ref.14
	Modified residue	314	1	Phosphohistidine Ref.12
	Modified residue	316	1	Phosphoserine Ref.13
	Modified residue	317	1	Phosphoserine Ref.14

Sequences

	Sequence		Length	Mass (Da)
	P25342 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 672467301D4D2697	FASTA	322	37,025
	10 20 30 40 50 60 MDPLSSVQPA SYVGFDTITN QIEHRLLKKG FQFNIMVVGQ SGLGKSTLIN TLFASHLIDS 70 80 90 100 110 120 ATGDDISALP VTKTTEMKIS THTLVEDRVR LNINVIDTPG FGDFIDNSKA WEPIVKYIKE 130 140 150 160 170 180 QHSQYLRKEL TAQRERFITD TRVHAILYFL QPNGKELSRL DVEALKRLTE IANVIPVIGK 190 200 210 220 230 240 SDTLTLDERT EFRELIQNEF EKYNFKIYPY DSEELTDEEL ELNRSVRSII PFAVVGSENE 250 260 270 280 290 300 IEINGETFRG RKTRWSAINV EDINQCDFVY LREFLIRTHL QDLIETTSYI HYEGFRARQL 310 320 IALKENANSR SSAHMSSNAI QR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the CDC10 region at chromosome III of Saccharomyces cerevisiae." Steensma H.Y., van der Aart Q.J.M. Yeast 7:425-429(1991) [PubMed: 1872033] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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: 8791410] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26109 / X2180.
[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: 9813094] [Abstract] Cited for: IDENTIFICATION IN THE SEPTIN COMPLEX.
[6]	"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: 12058072] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE GIN4 COMPLEX.
[7]	"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: 12665577] [Abstract] Cited for: ASSOCIATION WITH PHOSPHOINOSIDES LIPIDS, INTERACTION WITH CDC11.
[8]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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: 15282341] [Abstract] Cited for: SELF-ASSOCIATION, ASSEMBLY OF THE SEPTIN FILAMENTS.
[11]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, MASS SPECTROMETRY. Strain: ADR376.
[12]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT HIS-314, MASS SPECTROMETRY.
[13]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-316, MASS SPECTROMETRY.
[14]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-216; SER-311; SER-312 AND SER-317, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S48552 Genomic DNA. Translation: AAD13856.1. X59720 Genomic DNA. Translation: CAA42339.1. L16549 Genomic DNA. Translation: AAB49377.1. BK006937 Genomic DNA. Translation: DAA07481.1.
PIR	S19441.
RefSeq	NP_009928.1. NM_001178715.1.
3D structure databases
ProteinModelPortal	P25342.
SMR	P25342. Positions 29-301.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-673N.
IntAct	P25342. 18 interactions.
MINT	MINT-619481.
STRING	P25342.
Proteomic databases
PeptideAtlas	P25342.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCR002C; YCR002C; YCR002C.
GeneID	850358.
KEGG	sce:YCR002C.
NMPDR	fig|4932.3.peg.651.
Organism-specific databases
CYGD	YCR002c.
SGD	S000000595. CDC10.
Phylogenomic databases
eggNOG	fuNOG04134.
GeneTree	EFGT00050000003512.
HOGENOM	HBG715249.
OMA	RCWDPIV.
OrthoDB	EOG4HMNJX.
Gene expression databases
ArrayExpress	P25342.
Genevestigator	P25342.
GermOnline	YCR002C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000038. Cell_div_GTP-bd. IPR016491. Septin. [Graphical view]
PANTHER	PTHR18884. Cell_Div_GTP_bd. 1 hit.
Pfam	PF00735. Septin. 1 hit. [Graphical view]
PIRSF	PIRSF006698. Septin. 1 hit.
ProtoNet	Search...
Other
NextBio	965830.

Entry information

Entry name

CDC10_YEAST

Accession

Primary (citable) accession number: P25342
Secondary accession number(s): D6VR12

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program