For publication of results, please cite the following article: CPLA 1.0: an integrated database of protein lysine acetylation Zexian Liu , Xinjiao Gao, Jun Cao, Haiyan Liu, Yanhong Zhou, Longping Wen, Xiangjiao Yang, Xuebiao Yao, Jian Ren

For publication of results, please cite
the following article:

CPLA 1.0: an integrated database of protein lysine acetylation Zexian Liu , Xinjiao Gao, Jun Cao, Haiyan Liu, Yanhong Zhou, Longping Wen, Xiangjiao Yang, Xuebiao Yao, Jian Ren , Yu Xue . Nucleic Acids Research.2010.(Accepted )

There are two types of acetylation processes
widely occurred in proteins. The first Nα-terminal acetylation is
catalyzed a variety of N-terminal acetyltransferases (NATs), which
cotranslationally transfer acetyl moieties from acetyl-coenzyme A
(Acetyl-CoA) to the α-amino (Nα) group of protein amino-terminal
residues. Although Nα-terminal acetylation is rare in prokaryotes, it
was estimated that about 85% of eukaryotic proteins are Nα-terminally
modified (Polevoda et al
., 2000

; Polevoda et al
., 2002

). The second type is Nε-lysine acetylation, which specifically modifies ε-amino group of protein lysine residues (Yang et al
., 2007

; Shahbazian et al
., 2007

; Smith et al
., 2009

).
Although Nε-lysine acetylation is less common, it’s one of the most
important and ubiquitous post-translational modifications conserved in
prokaryotes and eukaryotes. Moreover, the acetylation and deacetylation
are dynamically and temporally regulated by histone acetyltransferases
(HATs) and histone deacetylases (HDACs), respectively (Yang et al
., 2004

; Lee et al
., 2007

).

In 1964, Allfrey et al. firstly observed that lysine
acetylation of histones plays an essential role in regulation of gene
expression (Allfrey et al
., 1964

).
Later and recent studies in epigenetics solidified this seminal
discovery, and proposed acetylation as a key component of the “histone
code” (Jenuwein et al
., 2001

).
Beyond histones, a wide range of non-histone proteins can also be
lysine acetylated, and involved in a variety of biological processes,
such as transcription regulation (Yuan et al
., 2005

), DNA replication (Terret et al
., 2009

; Choudhary et al
., 2009

), cellular signaling (Walkinshaw et al
., 2008

; Spange et al
., 2009

), stress response (Brunet et al
., 2004

) and so on. Aberrance of lysine acetylation and deacetylation is associated with various diseases and cancers (Kim et al
., 2006

). In particular, acetylation was demonstrated to be implicated in cellular metabolism and aging (Wang et al
., 2010

; Zhao et al
., 2010

), while one class of NAD+ dependent HDACs of sirtuins might be potent drug target for promoting longevity (Cohen et al
., 2004

; Wang et al
., 2010

).

Since the number of known acetylation sites is rapidly
increased, it is an urgent topic to collect the experimental data and
provide an integrated resource for the community. Recently, several
public databases, such as PhosphoSitePlus
, HPRD
, SysPTM
, and dbPTM
,
have already contained protein acetylation information. In these
databases, both of Nα-terminal and Nε-lysine acetylation data were
curated, while lysine acetylation sites are usually only a limited part
of total sites. So, thousands of lysine acetylation sites in other
species still remain to be collected.

Currently, the CPLA
1.0

database was updated on March 1st, 2010, containing
3,311


unique protein
entries with 7,151


lysine acetylation sites. The online service of CPLA 1.0 was implemented in PHP + MySQL
+ JavaScript. And the local packages of CPLA 1.0 were developed in
JAVA 1.5 (J2SE). The database will be updated routinely as new acetylated
lysines are reported.

The CPLA
1.0

supports Windows,
Unix/Linux and Mac and is freely available for academic
researches at: http://cpla.biocuckoo.org/

.