CPLM-005367

Genbank Nucleotide ID

Cell division control protein 10

Protein Synonyms/Alias

YCR002C; YCR022; YCR2C

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

Position	Peptide	Type	References
73	ISALPVTKTTEMKIS	acetylation	[1]
78	VTKTTEMKISTHTLV	acetylation	[1]
116	KAWEPIVKYIKEQHS	acetylation	[2]
119	EPIVKYIKEQHSQYL	acetylation	[2]
119	EPIVKYIKEQHSQYL	ubiquitination	[3]
128	QHSQYLRKELTAQRE	acetylation	[1, 4]
166	RLDVEALKRLTEIAN	acetylation	[1, 4]

[1] 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]
[2] 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]
[3] 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]
[4] 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]

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 39 46 GTP (By similarity).
NP_BIND 180 188 GTP (By similarity).
BINDING 74 74 GTP (By similarity).
BINDING 100 100 GTP; via amide nitrogen (By similarity).
BINDING 236 236 GTP; via amide nitrogen and carbonyl
BINDING 251 251 GTP (By similarity).
MOD_RES 216 216 Phosphothreonine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
GO:0001400; C:mating projection base; IDA:SGD.
GO:0043332; C:mating projection tip; IDA:SGD.
GO:0072687; C:meiotic spindle; IDA:SGD.
GO:0005628; C:prospore membrane; IDA:SGD.
GO:0031105; C:septin complex; IDA:SGD.
GO:0032160; C:septin filament array; IDA:SGD.
GO:0005876; C:spindle microtubule; 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; IDA:SGD.
GO:0000910; P:cytokinesis; IDA:SGD.
GO:0010458; P:exit from mitosis; IMP:SGD.
GO:0030011; P:maintenance of cell polarity; IC:SGD.
GO:0000921; P:septin ring assembly; IMP:SGD.
GO:0043934; P:sporulation; IDA:SGD.

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