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PR01224

Identifier
DELTATUBULIN  [View Relations]  [View Alignment]  
Accession
PR01224
No. of Motifs
12
Creation Date
02-DEC-1999
Title
Delta-tubulin signature
Database References
PRINTS; PR01161 TUBULIN
INTERPRO; IPR002967
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.CYTOSKELETON 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. TRABUCO, E.C. AND DUTCHER, S.K.
Uni3 tubulin.
UNPUBLISHED.
 
7. SMRZKA, O.W. AND BORNENS, M.
Intracellular distribution and function of a new delta type tubulin
in mammalian cells.
UNPUBLISHED.

Documentation
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, a new delta-type tubulin has been identified
in Chlamydomonas rheinhardtii [6] and mouse [7], and is likely to be found
in a number of other species.
 
DELTATUBULIN is a 12-element fingerprint that provides a signature for
delta-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 
delta-tubulins but distinguish them from the rest of the tubulin family.
A single iteration on SWALL19991110 was required to reach convergence, no 
further sequences being identified beyond the starting set. Several partial 
matches were also found, all of which are gamma- or alpha-tubulins that
match two motifs.
Summary Information
   2 codes involving 12 elements
0 codes involving 11 elements
0 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
8 codes involving 2 elements
Composite Feature Index
12222222222222
11000000000000
10000000000000
9000000000000
8000000000000
7000000000000
6000000000000
5000000000000
4000000000000
3000000000000
2000167000020
123456789101112
True Positives
AAD52009      O22416        
True Positive Partials
Codes involving 2 elements
AAC27620 Q9Z310 TBA2_EMENI TBAA_SCHCO
TBG1_DROME TBG_HUMAN TBG_XENLA TBG_YEAST
Sequence Titles
AAD52009    DELTA TUBULIN - Mus musculus (Mouse)          
O22416 TUBULIN UNI3 - CHLAMYDOMONAS REINHARDTII.

AAC27620 F GAMMA-TUBULIN (FRAGMENT) - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q9Z310 TUBULIN - RATTUS NORVEGICUS (RAT).
TBA2_EMENI TUBULIN ALPHA-2 CHAIN - EMERICELLA NIDULANS (ASPERGILLUS NIDULANS).
TBAA_SCHCO TUBULIN ALPHA-1A CHAIN - SCHIZOPHYLLUM COMMUNE (BRACKET FUNGUS).
TBG1_DROME TUBULIN GAMMA-1 CHAIN - DROSOPHILA MELANOGASTER (FRUIT FLY).
TBG_HUMAN TUBULIN GAMMA CHAIN - HOMO SAPIENS (HUMAN).
TBG_XENLA TUBULIN GAMMA CHAIN - XENOPUS LAEVIS (AFRICAN CLAWED FROG).
TBG_YEAST TUBULIN GAMMA CHAIN - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
Scan History
SWALL19991110 1  50   NSINGLE    
Initial Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
EPKVINQTLSKAAQSGRW AAD52009 69 69 -
EPKVVAGARSAAAASGSW O22416 60 60 -

Motif 2 width=11
Element Seqn Id St Int Rpt
YSVHGPKHEES AAD52009 108 21 -
FHGYGPQVHED O22416 100 22 -

Motif 3 width=12
Element Seqn Id St Int Rpt
YSSSLKMNQIIW AAD52009 162 43 -
YHSAFVANCCVW O22416 154 43 -

Motif 4 width=13
Element Seqn Id St Int Rpt
WPYGTGEVIVQNY AAD52009 173 -1 -
WPYESGEVIVQPY O22416 165 -1 -

Motif 5 width=21
Element Seqn Id St Int Rpt
NSILTLSHLYRSSDALLIHEN AAD52009 186 0 -
NTLLTLSHLADVSDGLVLLEN O22416 178 0 -

Motif 6 width=21
Element Seqn Id St Int Rpt
AVHKICAKRMNIKQISFRDLN AAD52009 208 1 -
ALHRTAAKLYGIARPSFGDMN O22416 200 1 -

Motif 7 width=21
Element Seqn Id St Int Rpt
DLMEHLVPHPEFKMLGVRNIP AAD52009 258 29 -
ELVTRLCGHPAYRLLTLRSVP O22416 340 119 -

Motif 8 width=23
Element Seqn Id St Int Rpt
FTWAGLLKHLRQMLISSAKMEEG AAD52009 290 11 -
FTWPALTKRLRQMLVTGSVLEEG O22416 372 11 -

Motif 9 width=20
Element Seqn Id St Int Rpt
EGFKDPALYTSWLEPVDAFS AAD52009 359 46 -
GEFADPALSAAWSPEPLSVS O22416 440 45 -

Motif 10 width=20
Element Seqn Id St Int Rpt
FDKYEKSAALVSNSQLLVKP AAD52009 386 7 -
FGRCAMSACLLSNDRHCVGP O22416 465 5 -

Motif 11 width=19
Element Seqn Id St Int Rpt
SSKAFIHQYTKFGMEEEDF AAD52009 418 12 -
ESRAFVHQYEKYGLSVAEF O22416 497 12 -

Motif 12 width=15
Element Seqn Id St Int Rpt
FLDSFALLEQVVASY AAD52009 436 -1 -
FQDCFARIEDIAQRY O22416 515 -1 -
Final Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
EPKVINQTLSKAAQSGRW AAD52009 69 69 -
EPKVVAGARSAAAASGSW O22416 60 60 -

Motif 2 width=11
Element Seqn Id St Int Rpt
YSVHGPKHEES AAD52009 108 21 -
FHGYGPQVHED O22416 100 22 -

Motif 3 width=12
Element Seqn Id St Int Rpt
YSSSLKMNQIIW AAD52009 162 43 -
YHSAFVANCCVW O22416 154 43 -

Motif 4 width=13
Element Seqn Id St Int Rpt
WPYGTGEVIVQNY AAD52009 173 -1 -
WPYESGEVIVQPY O22416 165 -1 -

Motif 5 width=21
Element Seqn Id St Int Rpt
NSILTLSHLYRSSDALLIHEN AAD52009 186 0 -
NTLLTLSHLADVSDGLVLLEN O22416 178 0 -

Motif 6 width=21
Element Seqn Id St Int Rpt
AVHKICAKRMNIKQISFRDLN AAD52009 208 1 -
ALHRTAAKLYGIARPSFGDMN O22416 200 1 -

Motif 7 width=21
Element Seqn Id St Int Rpt
DLMEHLVPHPEFKMLGVRNIP AAD52009 258 29 -
ELVTRLCGHPAYRLLTLRSVP O22416 340 119 -

Motif 8 width=23
Element Seqn Id St Int Rpt
FTWAGLLKHLRQMLISSAKMEEG AAD52009 290 11 -
FTWPALTKRLRQMLVTGSVLEEG O22416 372 11 -

Motif 9 width=20
Element Seqn Id St Int Rpt
EGFKDPALYTSWLEPVDAFS AAD52009 359 46 -
GEFADPALSAAWSPEPLSVS O22416 440 45 -

Motif 10 width=20
Element Seqn Id St Int Rpt
FDKYEKSAALVSNSQLLVKP AAD52009 386 7 -
FGRCAMSACLLSNDRHCVGP O22416 465 5 -

Motif 11 width=19
Element Seqn Id St Int Rpt
SSKAFIHQYTKFGMEEEDF AAD52009 418 12 -
ESRAFVHQYEKYGLSVAEF O22416 497 12 -

Motif 12 width=15
Element Seqn Id St Int Rpt
FLDSFALLEQVVASY AAD52009 436 -1 -
FQDCFARIEDIAQRY O22416 515 -1 -