Unknown

Dataset Information

0

Minimotif Miner 4: a million peptide minimotifs and counting.


ABSTRACT: Minimotif Miner (MnM) is a database and web system for analyzing short functional peptide motifs, termed minimotifs. We present an update to MnM growing the database from ?300 000 to >1 000 000 minimotif consensus sequences and instances. This growth comes largely from updating data from existing databases and annotation of articles with high-throughput approaches analyzing different types of post-translational modifications. Another update is mapping human proteins and their minimotifs to know human variants from the dbSNP, build 150. Now MnM 4 can be used to generate mechanistic hypotheses about how human genetic variation affect minimotifs and outcomes. One example of the utility of the combined minimotif/SNP tool identifies a loss of function missense SNP in a ubiquitylation minimotif encoded in the excision repair cross-complementing 2 (ERCC2) nucleotide excision repair gene. This SNP reaches genome wide significance for many types of cancer and the variant identified with MnM 4 reveals a more detailed mechanistic hypothesis concerning the role of ERCC2 in cancer. Other updates to the web system include a new architecture with migration of the web system and database to Docker containers for better performance and management. Weblinks:minimotifminer.org and mnm.engr.uconn.edu.

SUBMITTER: Lyon KF 

PROVIDER: S-EPMC5753208 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Minimotif Miner 4: a million peptide minimotifs and counting.

Lyon Kenneth F KF   Cai Xingyu X   Young Richard J RJ   Mamun Abdullah-Al AA   Rajasekaran Sanguthevar S   Schiller Martin R MR  

Nucleic acids research 20180101 D1


Minimotif Miner (MnM) is a database and web system for analyzing short functional peptide motifs, termed minimotifs. We present an update to MnM growing the database from ∼300 000 to >1 000 000 minimotif consensus sequences and instances. This growth comes largely from updating data from existing databases and annotation of articles with high-throughput approaches analyzing different types of post-translational modifications. Another update is mapping human proteins and their minimotifs to know  ...[more]

Similar Datasets

| S-EPMC2686579 | biostudies-literature
| S-EPMC2995834 | biostudies-literature
| S-EPMC4513861 | biostudies-literature
| S-EPMC5433680 | biostudies-literature
| S-EPMC6139474 | biostudies-literature
| S-EPMC2733157 | biostudies-literature
| S-EPMC2905367 | biostudies-other
| S-EPMC3517595 | biostudies-literature
| S-EPMC2924378 | biostudies-literature
| S-EPMC3319421 | biostudies-literature