Minimotif Miner: a tool for investigating protein function.
In addition to large domains, many short motifs mediate functional post-translational modification of proteins as well as protein-protein interactions and protein trafficking functions. We have constructed a motif database comprising 312 unique motifs and a web-based tool for identifying motifs in proteins. Functional motifs predicted by MnM can be ranked by several approaches, and we validated these scores by analyzing thousands of confirmed examples and by confirming prediction of previously unidentified 14-3-3 motifs in EFF-1.
Department of Computer Science and Engineering, University of Connecticut, Storrs, Connecticut 06269, USA.
Sudha
S
Balla
Vishal
V
Thapar
Snigdha
S
Verma
Thaibinh
T
Luong
Tanaz
T
Faghri
Chun-Hsi
CH
Huang
Sanguthevar
S
Rajasekaran
Jacob J
JJ
del Campo
Jessica H
JH
Shinn
William A
WA
Mohler
Mark W
MW
Maciejewski
Michael R
MR
Gryk
Bryan
B
Piccirillo
Stanley R
SR
Schiller
Martin R
MR
Schiller
D048948:14-3-3 Proteins / Q000737:chemistry / Q000502:physiology; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry / Q000502:physiology; D019992:Databases as Topic; D020407:Internet; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000502:physiology; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry / Q000502:physiology*; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein / Q000379:methods*; D012984:Software
D048948:14-3-3 Proteins; D029742:Caenorhabditis elegans Proteins; C470734:EFF-1 protein, C elegans; D008562:Membrane Glycoproteins; D011506:Proteins