Cell division control protein 12 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32468 (CDC12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cell division control protein 12

Alternative name(s):
Septin

Gene names

Name:	CDC12
Synonyms:	CLA10, PSL7
Ordered Locus Names:	YHR107C

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	407 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.7
Miscellaneous	Present with 1170 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
Domain	Coiled coil
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 maintenance of cell polarity Inferred from mutant phenotype. Source: SGD positive regulation of protein kinase activity Inferred from direct assay. Source: SGD septin ring assembly Inferred from mutant phenotype. Source: SGD
Cellular component	cellular bud neck septin ring Inferred from direct assay. Source: SGD mating projection Inferred from direct assay. Source: SGD membrane Inferred from electronic annotation. Source: UniProtKB-SubCell septin complex Inferred from direct assay. Source: SGD septin filament array Inferred from direct assay Ref.10. Source: SGD
Molecular function	1-phosphatidylinositol binding Inferred from direct assay Ref.8. Source: SGD GTP binding Inferred from direct assay. Source: SGD GTPase activity Inferred from direct assay. Source: SGD protein complex scaffold Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CDC11	P32458	10	EBI-4182,EBI-4178
GIC1	P38785	5	EBI-4182,EBI-7575
GIC2	Q06648	5	EBI-4182,EBI-7585
SHS1	Q07657	4	EBI-4182,EBI-22083
SPC24	Q04477	3	EBI-4182,EBI-27228

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 407

407

Cell division control protein 12

PRO_0000173500

Regions

Nucleotide binding

41 – 48

GTP By similarity

Nucleotide binding

180 – 188

GTP By similarity

Coiled coil

344 – 406

Potential

Sites

Binding site

GTP By similarity

Binding site

101

GTP; via amide nitrogen By similarity

Binding site

247

GTP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

263

GTP By similarity

Amino acid modifications

Modified residue

183

Phosphothreonine Ref.11

Modified residue

185

Phosphothreonine Ref.11

Modified residue

224

Phosphoserine Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P32468 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: A72DC393A6DBF924
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FASTA

407

46,668

        10         20         30         40         50         60 
MSAATATAAP VPPPVGISNL PNQRYKIVNE EGGTFTVMLC GESGLGKTTF INTLFQTVLK 

        70         80         90        100        110        120 
RADGQQHRQE PIRKTVEIDI TRALLEEKHF ELRVNVIDTP GFGDNVNNNK AWQPLVDFID 

       130        140        150        160        170        180 
DQHDSYMRQE QQPYRTKKFD LRVHAVLYFI RPTGHGLKPI DIETMKRLST RANLIPVIAK 

       190        200        210        220        230        240 
ADTLTAQELQ QFKSRIRQVI EAQEIRIFTP PLDADSKEDA KSGSNPDSAA VEHARQLIEA 

       250        260        270        280        290        300 
MPFAIVGSEK KFDNGQGTQV VARKYPWGLV EIENDSHCDF RKLRALLLRT YLLDLISTTQ 

       310        320        330        340        350        360 
EMHYETYRRL RLEGHENTGE GNEDFTLPAI APARKLSHNP RYKEEENALK KYFTDQVKAE 

       370        380        390        400 
EQRFRQWEQN IVNERIRLNG DLEEIQGKVK KLEEQVKSLQ VKKSHLK

« Hide

References

	« Hide 'large scale' referencesShow '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: 8791410] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204510 / AB320.
[2]	"Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast." Cvrckova F., de Virgilio C., Manser E., Pringle J.R., Nasmyth K. Genes Dev. 9:1817-1830(1995) [PubMed: 7649470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K1107.
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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]	"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].
[8]	"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.
[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]	"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 THR-183 AND THR-185, MASS SPECTROMETRY.
[12]	"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-224, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L16551 Genomic DNA. Translation: AAB50036.1. X82498 Genomic DNA. Translation: CAA57878.1. U00059 Genomic DNA. Translation: AAB68863.1. BK006934 Genomic DNA. Translation: DAA06801.1.
PIR	S50870.
RefSeq	NP_011975.1. NM_001179237.1.
3D structure databases
ProteinModelPortal	P32468.
SMR	P32468. Positions 33-314.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-853N.
IntAct	P32468. 37 interactions.
MINT	MINT-434899.
STRING	P32468.
Proteomic databases
PeptideAtlas	P32468.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR107C; YHR107C; YHR107C.
GeneID	856507.
KEGG	sce:YHR107C.
NMPDR	fig\|4932.3.peg.3136.
Organism-specific databases
CYGD	YHR107c.
SGD	S000001149. CDC12.
Phylogenomic databases
eggNOG	fuNOG04451.
GeneTree	EFGT00050000003512.
HOGENOM	HBG715249.
OMA	CDFKKLR.
OrthoDB	EOG4JDMG9.
Gene expression databases
ArrayExpress	P32468.
Genevestigator	P32468.
GermOnline	YHR107C. 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	982239.

Entry information

Entry name

CDC12_YEAST

Accession

Primary (citable) accession number: P32468
Secondary accession number(s): D3DL57

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	December 14, 2011
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VIII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents