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PR01519

Identifier
EPSLNTUBULIN  [View Relations]  [View Alignment]  
Accession
PR01519
No. of Motifs
10
Creation Date
28-JUN-2001
Title
Epsilon-tubulin signature
Database References
PRINTS; PR01161 TUBULIN
Literature References
1. CLEVELAND, D.W. AND SULLIVAN, K.F. 
Molecular biology and genetics of tubulin. 
ANNU.REV.BIOCHEMISTRY 54 331-365 (1985).
 
2. JOSHI, H.C. AND CLEVELAND, D.W. 
Diversity among tubulin subunits: toward what functional end? 
CELL MOTIL.CYTOSKEL. 16 159-163 (1990).
 
3. MITCHISON, T.J. 
Localization of an exchangeable GTP binding site at the plus end of
microtubules. 
SCIENCE 261 1044-1047 (1993).
 
4. HESSE, J., THIERAUF, M. AND PONSTINGL, H. 
Tubulin sequence region beta 155-174 is involved in binding exchangeable 
guanosine triphosphate.
J.BIOL.CHEM. 262 15472-15475 (1987).
 
5. JOSHI, H.C. 
Gamma-tubulin: the hub of cellular microtubule assemblies.
BIOESSAYS 15 637-643 (1993).
 
6. CHANG, P. AND STEARNS, T. 
Delta-tubulin and epsilon-tubulin: two new human centrosomal tubulins reveal
new aspects of centrosome structure and function.
NAT.CELL BIOL. 2 30-35 (2000).
 
7. VAUGHAN, S., ATTWOOD, T., NAVARRO, M., SCOTT, V., MCKEAN, P. AND GULL, K.
New tubulins in protozoal parasites. 
CURR.BIOL. 10 R258-258 (2000).

Documentation
PRINTS; PR01164 GAMMATUBULIN; PR01224 DELTATUBULIN; PR01520 ZETATUBULIN
Microtubules are polymers of tubulin, a dimer of two 55kDa subunits,
designated alpha and beta [1,2]. Within the microtubule lattice, alpha-beta
heterodimers associate in a head-to-tail fashion, giving rise to microtubule 
polarity. Fluorescent labelling studies have suggested that tubulin is
oriented in microtubules with beta-tubulin toward the plus end [3].
 
For maximal rate and extent of polymerisation into microtubules, tubulin
requires GTP. Two molecules of GTP are bound at different sites, termed N
and E. At the E (Exchangeable) site, GTP is hydrolysed during incorporation
into the microtubule. Close to the E site is an invariant region rich in
glycine residues, which is found in both chains and is thought to control
access of the nucleotide to its binding site [4].
 
Most species, excepting simple eukaryotes, express a variety of closely-
related alpha- and beta-isotypes. A third family member, gamma-tubulin, has
also been identified in a number of species. Gamma-tubulin is found at
microtubule-organising centres, such as the spindle poles or the centrosome, 
suggesting that it is involved in minus-end nucleation of microtubule
assembly [5]. More recently, epsilon-tubulin has been identified in humans 
[6] and Trypanosomes [7]; in humans, it has been localised to centrosomes [6].
 
EPSLNTUBULIN is a 10-element fingerprint that provides a signature for the
epsilon-tubulins. The fingerprint was derived from an initial alignment of 2
sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, focusing on those sections that characterise the
epsilon-tubulins but distinguish them from the rest of the tubulin family. 
A single iteration on SPTR39_8-15_10 was required to reach convergence, no 
further sequences being identified beyond the starting set. Several partial
matches were found, all of which are alpha-, beta- or gamma-tubulins that
match two motifs.
Summary Information
   2 codes involving 10 elements
0 codes involving 9 elements
0 codes involving 8 elements
0 codes involving 7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
7 codes involving 2 elements
Composite Feature Index
102222222222
90000000000
80000000000
70000000000
60000000000
50000000000
40000000000
30000000000
21204012301
12345678910
True Positives
Q9NI44        TBE_HUMAN     
True Positive Partials
Codes involving 2 elements
P79008 Q94771 Q9VT30 TBA2_SCHPO
TBA4_DROME TBB1_PORPU TBB1_SOYBN
Sequence Titles
Q9NI44      EPSILON TUBULIN - Trypanosoma brucei.         
TBE_HUMAN TUBULIN EPSILON CHAIN (EPSILON TUBULIN) - Homo sapiens (Human).

P79008 BETA1-TUBULIN - Coprinus cinereus (Inky cap fungus).
Q94771 GAMMA-TUBULIN - Trypanosoma brucei brucei.
Q9VT30 ALPHATUB67C PROTEIN - Drosophila melanogaster (Fruit fly).
TBA2_SCHPO TUBULIN ALPHA-2 CHAIN - Schizosaccharomyces pombe (Fission yeast).
TBA4_DROME TUBULIN ALPHA-4 CHAIN - Drosophila melanogaster (Fruit fly).
TBB1_PORPU TUBULIN BETA-1 CHAIN - Porphyra purpurea.
TBB1_SOYBN TUBULIN BETA-1 CHAIN - Glycine max (Soybean).
Scan History
SPTR39_8-15_10 1  50   NSINGLE    
Initial Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
DMEEGVLRAMLRGP Q9NI44 72 72 -
DMEEGVVNEILQGP TBE_HUMAN 75 75 -

Motif 2 width=19
Element Seqn Id St Int Rpt
PLRDVFDTKQLITDISGSG TBE_HUMAN 88 -1 -
PLGHLFDATFFVSDVSGAG Q9NI44 85 -1 -

Motif 3 width=19
Element Seqn Id St Int Rpt
WAVGHMEYGDKYIDSITET Q9NI44 106 2 -
WAVGHKVFGSLYQDQILEK TBE_HUMAN 109 2 -

Motif 4 width=20
Element Seqn Id St Int Rpt
EQVERCDSIQSFLIMHSLSG Q9NI44 127 2 -
KSAEHCDCLQCFFIIHSMGG TBE_HUMAN 130 2 -

Motif 5 width=23
Element Seqn Id St Int Rpt
GTRVLGMLEDEFPHVFRICPVVM Q9NI44 153 6 -
GTFLLKVLEDEFPEVYRFVTSIY TBE_HUMAN 156 6 -

Motif 6 width=18
Element Seqn Id St Int Rpt
PSGEDDVITSPYNSILAM TBE_HUMAN 179 0 -
PSAIDDVVTAPYNTAFAV Q9NI44 176 0 -

Motif 7 width=16
Element Seqn Id St Int Rpt
KELNEHADCVLPIDNQ TBE_HUMAN 197 0 -
RELIEHADAVLPLDND Q9NI44 194 0 -

Motif 8 width=21
Element Seqn Id St Int Rpt
RFEGSLNMDLNEISMNLVPFP TBE_HUMAN 274 61 -
RFPGPLNMDINEITTNLVPYP Q9NI44 277 67 -

Motif 9 width=21
Element Seqn Id St Int Rpt
RNIERLKPSLQFVSWNQEGWK TBE_HUMAN 361 66 -
RNIPRIRERQKLVYWNEDGCK Q9NI44 374 76 -

Motif 10 width=20
Element Seqn Id St Int Rpt
MELKERFMRLYKKKAHLHHY TBE_HUMAN 410 28 -
QSAHERFMRLYSVRSHVHHY Q9NI44 423 28 -
Final Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
DMEEGVLRAMLRGP Q9NI44 72 72 -
DMEEGVVNEILQGP TBE_HUMAN 75 75 -

Motif 2 width=19
Element Seqn Id St Int Rpt
PLRDVFDTKQLITDISGSG TBE_HUMAN 88 -1 -
PLGHLFDATFFVSDVSGAG Q9NI44 85 -1 -

Motif 3 width=19
Element Seqn Id St Int Rpt
WAVGHMEYGDKYIDSITET Q9NI44 106 2 -
WAVGHKVFGSLYQDQILEK TBE_HUMAN 109 2 -

Motif 4 width=20
Element Seqn Id St Int Rpt
EQVERCDSIQSFLIMHSLSG Q9NI44 127 2 -
KSAEHCDCLQCFFIIHSMGG TBE_HUMAN 130 2 -

Motif 5 width=23
Element Seqn Id St Int Rpt
GTRVLGMLEDEFPHVFRICPVVM Q9NI44 153 6 -
GTFLLKVLEDEFPEVYRFVTSIY TBE_HUMAN 156 6 -

Motif 6 width=18
Element Seqn Id St Int Rpt
PSGEDDVITSPYNSILAM TBE_HUMAN 179 0 -
PSAIDDVVTAPYNTAFAV Q9NI44 176 0 -

Motif 7 width=16
Element Seqn Id St Int Rpt
KELNEHADCVLPIDNQ TBE_HUMAN 197 0 -
RELIEHADAVLPLDND Q9NI44 194 0 -

Motif 8 width=21
Element Seqn Id St Int Rpt
RFEGSLNMDLNEISMNLVPFP TBE_HUMAN 274 61 -
RFPGPLNMDINEITTNLVPYP Q9NI44 277 67 -

Motif 9 width=21
Element Seqn Id St Int Rpt
RNIERLKPSLQFVSWNQEGWK TBE_HUMAN 361 66 -
RNIPRIRERQKLVYWNEDGCK Q9NI44 374 76 -

Motif 10 width=20
Element Seqn Id St Int Rpt
MELKERFMRLYKKKAHLHHY TBE_HUMAN 410 28 -
QSAHERFMRLYSVRSHVHHY Q9NI44 423 28 -