SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR01740

Identifier
SEPTIN2  [View Relations]  [View Alignment]  
Accession
PR01740
No. of Motifs
3
Creation Date
27-JUN-2002
Title
Septin 2 signature
Database References
Literature References
1. HARTWELL, L.
Genetic control of the cell division cycle in yeast. IV. Genes controlling
bud emergence and cytokinesis.
EXP.CELL RES. 69 265-276 (1971).
 
2. HAARER, B. AND PRINGLE, J.
Immunofluorescence localization of the Saccharomyces cerevisiae CDC12 gene 
product to the vicinity of the 10-nm filaments in the mother-bud neck.
MOL.CELL BIOL. 7 3678-3687 (1987).
 
3. LONGTINE, M., THEESFELD, C., MCMILLAN, J., WEAVER, E., PRINGLE, J.
AND LEW, D.
Septin-dependent assembly of a cell cycle-regulatory module in 
Saccharomyces cerevisiae. 
MOL.CELL BIOL. 20 4049-4061 (2000).
 
4. FIELD, C. AND KELLOG, D.
Septins: cytoskeletal polymers or signalling GTPases? 
TRENDS CELL BIOL. 9 387-394 (1999).
 
5. BEITES, C., XIE, H., BOWSER, R. AND TRIMBLE, W.
The septin CDCrel-1 binds syntaxin and inhibits exocytosis.
NAT.NEUROSCI. 2 434-439. (1999).
 
6. KINOSHITA, M. AND NODA, M.
Roles of septins in the mammalian cytokinesis machinery.
CELL STRUCT.FUNCT. 26 667-670 (2001).
 
7. KINOSHITA, M., KUMAR, S., MIZOGUCHI, A., IDE, C., KINOSHITA, A., 
HARAGUCHI, T., HIRAOKA, Y. AND NODA, M.
Nedd5, a mammalian septin, is a novel cytoskeletal component interacting 
with actin-based structures.
GENES DEV. 11 1535-1547 (1997).

Documentation
Septins constitute a eukaryotic family of guanine nucleotide-binding proteins.
Members of the family were first identified by genetic screening for 
Saccharomyces cerevisiae mutants defective in cytokinesis [1]. Temperature-
sensitive mutations in four genes, CDC3, CDC10, CDC11 and CDC12, were found
to cause cell-cycle arrest and defects in bud growth and cytokinesis. The
protein products of these genes localise at the division plane between
mother and daughter cells, indicating a role in mother-daughter separation
during cytokinesis [2]. Members of the family were therefore termed septins
to reflect their role in septation and cell division. The identification of
septin homologues in higher eukaryotes, which localise to the cleavage
furrow in dividing cells, supports an orthologous function in cytokinesis.
Septins have since been identified in most eukaryotes, except plants [3].
 
Septins are approximately 40-50kDa in molecular mass, and typically comprise
a conserved central core domain (>35% sequence identity between mammalian
and yeast homologues) flanked by more divergent N- and C-termini. Most
septins possess a P-loop motif in their N-terminal domain (which is
characteristic of GTP-binding proteins), and a predicted C-terminal coiled-
coil domain [4].
 
A number of septin interaction partners have been identified in yeast, 
many of which are components of the budding site selection machinery, kinase
cascades or of the ubiquitination pathway [3,4]. It has therefore been 
proposed that septins may act as a scaffold that provides an interaction 
matrix for other proteins. In mammals, septins have been shown to interact
regulate vesicle dynamics [5]. Mammalian septins have also been implicated
in a variety of other cellular processes, including apoptosis, carcinogenesis
and neurodegeneration [6].
 
Septin 2, also termed NEDD5, was originally cloned in mice [7]. Orthlogues
from several other species have also been identified. Micro-injection of 
cells with an anti-septin 2 antibody blocks cytokinesis, giving rise to 
binucleated cells [7].
 
SEPTIN2 is a 3-element fingerprint that provides a signature for septin 2
proteins. The fingerprint was derived from an initial alignment of 3
sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, focusing on those sections that characterise 
septin 2 but distinguish it from other family members - all motifs lie
between the GTP-binding region and the putative coilded-coil domain. Two 
iterations on SPTR40_20f were required to reach convergence, at which point
a true set comprising 5 sequences was identified. 
Summary Information
5 codes involving  3 elements
0 codes involving 2 elements
Composite Feature Index
3555
2000
123
True Positives
Q91Y81        Q96CB0        Q9DE33        SEP2_HUMAN    
SEP2_MOUSE
Sequence Titles
Q91Y81      VASCULAR ENDOTHELIAL CELL SPECIFIC PROTEIN 11 - Rattus norvegicus (Rat). 
Q96CB0 SIMILAR TO NEURAL CELL EXPRESSED, DEVELOPMENTALLY DOWN-REGULATED 5 - Homo sapiens (Human).
Q9DE33 SEPTIN A - Xenopus laevis (African clawed frog).
SEP2_HUMAN Septin 2 (NEDD5 protein homolog) - Homo sapiens (Human).
SEP2_MOUSE Septin 2 (NEDD5 protein) - Mus musculus (Mouse).
Scan History
SPTR40_20f 2  250  NSINGLE    
Initial Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
PGAAEKIERTVQIEASTV Q91Y81 69 69 -
PGAAEKIERTVQIEASTV SEP2_MOUSE 69 69 -
PGAAEKIERTVQIEASTV SEP2_HUMAN 69 69 -

Motif 2 width=9
Element Seqn Id St Int Rpt
LKERERLKK Q91Y81 189 102 -
LKERERLKK SEP2_MOUSE 189 102 -
LKERERLKK SEP2_HUMAN 189 102 -

Motif 3 width=11
Element Seqn Id St Int Rpt
EQTRLLKASIP Q91Y81 226 28 -
EQTRLLKASIP SEP2_MOUSE 226 28 -
EQTRLLKASIP SEP2_HUMAN 226 28 -
Final Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
PGAAEKIERTVQIEASTV Q91Y81 69 69 -
PGAAEKIERTVQIEASTV SEP2_MOUSE 69 69 -
PGAAEKIERTVQIEASTV SEP2_HUMAN 69 69 -
SGAAEKIERTVQIEASTV Q96CB0 69 69 -
PGAADKIERTVDIEASTV Q9DE33 68 68 -

Motif 2 width=9
Element Seqn Id St Int Rpt
LKERERLKK Q91Y81 189 102 -
LKERERLKK SEP2_MOUSE 189 102 -
LKERERLKK SEP2_HUMAN 189 102 -
LKERERLKK Q96CB0 189 102 -
LRERERLKR Q9DE33 188 102 -

Motif 3 width=11
Element Seqn Id St Int Rpt
EQTRLLKASIP Q91Y81 226 28 -
EQTRLLKASIP SEP2_MOUSE 226 28 -
EQTRLLKASIP SEP2_HUMAN 226 28 -
EQTRLLKASIP Q96CB0 226 28 -
EQTRLLKASIP Q9DE33 225 28 -