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.
Balla
Sudha
S
Department of Computer Science and Engineering, University of Connecticut, Storrs, Connecticut 06269, USA.
Thapar
Vishal
V
Verma
Snigdha
S
Luong
Thaibinh
T
Faghri
Tanaz
T
Huang
Chun-Hsi
CH
Rajasekaran
Sanguthevar
S
del Campo
Jacob J
JJ
Shinn
Jessica H
JH
Mohler
William A
WA
Maciejewski
Mark W
MW
Gryk
Michael R
MR
Piccirillo
Bryan
B
Schiller
Stanley R
SR
Schiller
Martin R
MR
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