CPLM-006135

Genbank Nucleotide ID

Cell division control protein 12

Protein Synonyms/Alias

CLA10; PSL7; YHR107C

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

Position	Peptide	Type	References
88	TRALLEEKHFELRVN	acetylation	[1]
193	AQELQQFKSRIRQVI	acetylation	[2]
251	AIVGSEKKFDNGQGT	acetylation	[2, 3]
338	APARKLSHNPRYKEE	acetylation	[2]
351	EEENALKKYFTDQVK	ubiquitination	[4]

[1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
[2] Regulation of septin dynamics by the Saccharomyces cerevisiae lysine acetyltransferase NuA4.
Mitchell L, Lau A, Lambert JP, Zhou H, Fong Y, Couture JF, Figeys D, Baetz K.
PLoS One. 2011;6(10):e25336. [PMID: 21984913]
[3] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
[4] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]

Functional Description

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.

NP_BIND 41 48 GTP (By similarity).
NP_BIND 180 188 GTP (By similarity).
BINDING 75 75 GTP (By similarity).
BINDING 101 101 GTP; via amide nitrogen (By similarity).
BINDING 247 247 GTP; via amide nitrogen and carbonyl
BINDING 263 263 GTP (By similarity).

Cell cycle; Cell division; Coiled coil; Complete proteome; GTP-binding; Membrane; Nucleotide-binding; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
GO:0005937; C:mating projection; IDA:SGD.
GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO:0031105; C:septin complex; IDA:SGD.
GO:0032160; C:septin filament array; IDA:SGD.
GO:0005545; F:1-phosphatidylinositol binding; IDA:SGD.
GO:0005525; F:GTP binding; IDA:SGD.
GO:0003924; F:GTPase activity; IDA:SGD.
GO:0032947; F:protein complex scaffold; IMP:SGD.
GO:0000910; P:cytokinesis; IDA:SGD.
GO:0030011; P:maintenance of cell polarity; IMP:SGD.
GO:0045860; P:positive regulation of protein kinase activity; IDA:SGD.
GO:0000921; P:septin ring assembly; IMP:SGD.

IPR000038; Cell_div_GTP-bd.
IPR027417; P-loop_NTPase.
IPR016491; Septin.