SCUD: Saccharomyces Cerevisiae Ubiquitination Database

被引:29
作者
Lee, Won-Chul [1 ,2 ]
Lee, Minho [2 ]
Jung, Jin Woo [1 ]
Kim, Kwang Pyo [1 ,3 ]
Kim, Dongsup [2 ]
机构
[1] Konkuk Univ, Dept Mol Biotechnol, Seoul 143701, South Korea
[2] Korea Adv Inst Sci & Technol, Dept Bio & Brain Engn, Taejon 305701, South Korea
[3] Konkuk Univ, Inst Biomed Sci & Technol, Seoul 143701, South Korea
关键词
D O I
10.1186/1471-2164-9-440
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Background: Ubiquitination is an important post-translational modification involved in diverse biological processes. Therefore, genomewide representation of the ubiquitination system for a species is important. Description: SCUD is a web-based database for the ubiquitination system in Saccharomyces cerevisiae ( Baker's yeast). We first searched for all the known enzymes involved in the ubiquitination process in yeast, including E1, E2, E3, and deubiquitination enzymes. Then, ubiquitinated substrates were collected by literature search. Especially, E3 and deubiquitination enzymes are classified into classes and subclasses by their shared domains and unique functions. As a result, 42 different E3 enzymes were grouped into corresponding classes and subclasses, and 940 ubiquitinated substrates including mutant substrates were identified. All the enzyme and substrate information are interconnected by hyperlinks, which makes it easy to view the enzyme-specific ubiquitination information. Conclusion: This database aims to represent a comprehensive yeast ubiquitination system, and is easily expandable with the further experimental data. We expect that this database will be useful for the research on the ubiquitination systems of other higher organisms. SCUD is accessible at http://scud.kaist.ac.kr
引用
收藏
页数:7
相关论文
共 11 条
[1]   UbiProt: a database of ubiquitylated proteins [J].
Chernorudskiy, Alexander L. ;
Garcia, Alejandro ;
Eremin, Eugene V. ;
Shorina, Anastasia S. ;
Kondratieva, Ekaterina V. ;
Gainullin, Murat R. .
BMC BIOINFORMATICS, 2007, 8 (1)
[2]   U-box proteins as a new family of ubiquitin ligases [J].
Hatakeyama, S ;
Nakayama, KI .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 302 (04) :635-645
[3]   A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery [J].
Hitchcock, AL ;
Auld, K ;
Gygi, SP ;
Silver, PA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (22) :12735-12740
[4]   A FAMILY OF PROTEINS STRUCTURALLY AND FUNCTIONALLY RELATED TO THE E6-AP UBIQUITIN-PROTEIN LIGASE (VOL 92, PG 2563, 1995) [J].
HUIBREGTSE, JM ;
SCHEFFNER, M ;
BEAUDENON, S ;
HOWLEY, PM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (11) :5249-5249
[5]   RING finger proteins: Mediators of ubiquitin ligase activity [J].
Joazeiro, CAP ;
Weissman, AM .
CELL, 2000, 102 (05) :549-552
[6]   A PROTEOLYTIC PATHWAY THAT RECOGNIZES UBIQUITIN AS A DEGRADATION SIGNAL [J].
JOHNSON, ES ;
MA, PCM ;
OTA, IM ;
VARSHAVSKY, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (29) :17442-17456
[7]   A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly [J].
Koegl, M ;
Hoppe, T ;
Schlenker, S ;
Ulrich, HD ;
Mayer, TU ;
Jentsch, S .
CELL, 1999, 96 (05) :635-644
[8]   For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection [J].
Kostova, Z ;
Wolf, DH .
EMBO JOURNAL, 2003, 22 (10) :2309-2317
[9]   A high throughput screen to identify substrates for the ubiquitin ligase Rsp5 [J].
Kus, B ;
Gajadhar, A ;
Stanger, K ;
Cho, R ;
Sun, W ;
Rouleau, N ;
Lee, T ;
Chan, D ;
Wolting, C ;
Edwards, A ;
Bosse, R ;
Rotin, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (33) :29470-29478
[10]   Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets [J].
Mayor, T ;
Lipford, JR ;
Graumann, J ;
Smith, GT ;
Deshaies, RJ .
MOLECULAR & CELLULAR PROTEOMICS, 2005, 4 (06) :741-751