dbPTM

EAF7_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EAF7_SCHPO
UniProt AC	O42924
Protein Name	Probable chromatin modification-related protein eaf7
Gene Name	eaf7
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	272
Subcellular Localization	Nucleus .
Protein Description	Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity)..
Protein Sequence	MSSRGTRSSTAAEQKRQEDVNKESNMNDSVTEWSVLEETLLLKAICRGLRPVGIEKNFYMIGILREIRDGCKRSTIKAQDVWNKLGTLYNLKEFEELEAPGNEEVKAKEKRIKSPDVKDFKLPKDILKVKEKSEKPLETSQKVEIETVETKPGEPEVKQETNLQKEKKESKVKLESKEEKISRNLRSSSRSISPVTEQPQSPKIQPVIPEKKEKSEKKESSMTLRKRSVSPSSQNTARSPKRMATEPIEPASSPAASNQAIRRSSRSRRPPT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
114	Phosphorylation	AKEKRIKSPDVKDFK HHHHHCCCCCHHHCC	24.78	25720772
187	Phosphorylation	KISRNLRSSSRSISP HHHHHHHHCCCCCCC	35.51	25720772
188	Phosphorylation	ISRNLRSSSRSISPV HHHHHHHCCCCCCCC	24.28	21712547
189	Phosphorylation	SRNLRSSSRSISPVT HHHHHHCCCCCCCCC	31.15	25720772
191	Phosphorylation	NLRSSSRSISPVTEQ HHHHCCCCCCCCCCC	29.39	25720772
193	Phosphorylation	RSSSRSISPVTEQPQ HHCCCCCCCCCCCCC	17.98	28889911
196	Phosphorylation	SRSISPVTEQPQSPK CCCCCCCCCCCCCCC	32.08	25720772
201	Phosphorylation	PVTEQPQSPKIQPVI CCCCCCCCCCCCCCC	34.54	28889911
228	Phosphorylation	SMTLRKRSVSPSSQN CCCHHHHCCCHHHHC	29.95	24763107
230	Phosphorylation	TLRKRSVSPSSQNTA CHHHHCCCHHHHCCC	21.95	28889911
232	Phosphorylation	RKRSVSPSSQNTARS HHHCCCHHHHCCCCC	36.73	25720772
233	Phosphorylation	KRSVSPSSQNTARSP HHCCCHHHHCCCCCC	30.73	21712547
236	Phosphorylation	VSPSSQNTARSPKRM CCHHHHCCCCCCCCC	18.79	21712547
239	Phosphorylation	SSQNTARSPKRMATE HHHCCCCCCCCCCCC	32.10	24763107
245	Phosphorylation	RSPKRMATEPIEPAS CCCCCCCCCCCCCCC	32.71	29996109
252	Phosphorylation	TEPIEPASSPAASNQ CCCCCCCCCHHHHHH	47.79	29996109
253	Phosphorylation	EPIEPASSPAASNQA CCCCCCCCHHHHHHH	22.21	25720772
257	Phosphorylation	PASSPAASNQAIRRS CCCCHHHHHHHHHHH	31.42	29996109

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of EAF7_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EAF7_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EAF7_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EAF7_SCHPO !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EAF7_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-201, ANDMASS SPECTROMETRY.	18257517 [Abstract]