CPLM-006128

Genbank Nucleotide ID

Cell division control protein 3

Protein Synonyms/Alias

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

Position	Peptide	Type	References
4	****MSLKEEQVSIK	acetylation	[1, 2]
4	****MSLKEEQVSIK	sumoylation	[3, 4, 5]
11	KEEQVSIKQDPEQEE	sumoylation	[3, 4, 5]
11	KEEQVSIKQDPEQEE	ubiquitination	[5, 6]
30	QFNDVQIKQESQDHD	sumoylation	[3, 4, 5]
30	QFNDVQIKQESQDHD	ubiquitination	[5]
63	EAAESDVKVEPGLGM	sumoylation	[3, 4, 5, 7]
63	EAAESDVKVEPGLGM	ubiquitination	[5]
137	IGKTTLMKTLFNNDD	acetylation	[1]
239	QYLDAENKINRHSIN	acetylation	[8]
287	NLIPVIAKSDILTDE	sumoylation	[4]
316	QSNIELFKPPIYSND	acetylation	[1]
415	KLAKLGIKQDNSVFK	ubiquitination	[6]
443	LHEAKLAKLEIEMKT	sumoylation	[4]
465	EKEKKLQKSETELFA	sumoylation	[4]
514	NHSPVPTKKKGFLR*	ubiquitination	[6]

[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] 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]
[3] Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin.
Rallabhandi P, Hashimoto K, Mo YY, Beck WT, Moitra PK, D'Arpa P.
J Biol Chem. 2002 Oct 18;277(42):40020-6. [PMID: 12149243]
[4] Comparative analysis of yeast PIAS-type SUMO ligases in vivo and in vitro.
Takahashi Y, Toh-E A, Kikuchi Y.
J Biochem. 2003 Apr;133(4):415-22. [PMID: 12761287]
[5] Cytoplasmic sumoylation by PIAS-type Siz1-SUMO ligase.
Takahashi Y, Iwase M, Strunnikov AV, Kikuchi Y.
Cell Cycle. 2008 Jun 15;7(12):1738-44. [PMID: 18583943]
[6] 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]
[7] A proteomic strategy for gaining insights into protein sumoylation in yeast.
Denison C, Rudner AD, Gerber SA, Bakalarski CE, Moazed D, Gygi SP.
Mol Cell Proteomics. 2005 Mar;4(3):246-54. [PMID: 15542864]
[8] 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]

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 126 133 GTP (By similarity).
NP_BIND 287 295 GTP (By similarity).
BINDING 207 207 GTP; via amide nitrogen (By similarity).
BINDING 344 344 GTP; via amide nitrogen and carbonyl
BINDING 360 360 GTP (By similarity).
MOD_RES 2 2 N-acetylserine.
MOD_RES 2 2 Phosphoserine.
MOD_RES 9 9 Phosphoserine.
MOD_RES 47 47 Phosphothreonine.
MOD_RES 60 60 Phosphoserine.
MOD_RES 77 77 Phosphoserine.
MOD_RES 175 175 Phosphoserine.
MOD_RES 468 468 Phosphothreonine.
MOD_RES 509 509 Phosphoserine.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 287 287 Glycyl lysine isopeptide (Lys-Gly)

Acetylation; Cell cycle; Cell division; Coiled coil; Complete proteome; GTP-binding; Isopeptide bond; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005619; C:ascospore wall; IDA:SGD.
GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
GO:0001400; C:mating projection base; 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:0005545; F:1-phosphatidylinositol binding; IDA:SGD.
GO:0005525; F:GTP binding; IDA:SGD.
GO:0005198; F:structural molecule activity; IDA:SGD.
GO:0000910; P:cytokinesis; IDA:SGD.
GO:0030011; P:maintenance of cell polarity; IC:SGD.
GO:0000921; P:septin ring assembly; IMP:SGD.
GO:0031107; P:septin ring disassembly; IMP:SGD.

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