dbPTM

EAF_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EAF_SCHPO
UniProt AC	O59773
Protein Name	Chromatin modification-related protein vid21
Gene Name	vid21
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	994
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	MKQKETKTSQIALVDGEKLSITDSFASLFTLDEEEENDSVDNEEIKLTKEKHEKLLLLFWLHCKFPNGLEWLHSSSDLLPEQVSEWFNFYQKYRFKRGRNFNLSARESVTPIVEEPIVPEEPDNLEGVSEETPLKETSLELSEEEIITSKSPIPSPETIHKNIDVEEKETIEPTTPVKEVETTAHAEEEKGPLTPDSEYAARQLTEELANKSSQEEGVDKQLRVVEATEKEHEEDGNEENVTVTKPVEVATDQVESKEVKKKEVSETTEPTAPPVTVAEVLEIEDKVPKVDEVEEVHSPEAKVTENDVENVQSGIDIEKTIQLLNNQEIPSEQQIISVDKATESPVQEVAVDVNEKPVDEIVEPSKLQMENKLPSEKSPTIDRTGVEAPLFELSVSMPLTLIPPSKFSEPVKPELSSEAWLLRTEMSPLHLRLKNAHKYVLSDNWSHAYREEIVRQSLHHLTVAKEKGIWSFRQPKRQNEMPRLKTHRDYVLDEMQWMSIDFSQERKWKIILAHRMANWVMDYHQASDKCTVCTPASLSKNKKPYMQENEHQKDSHEETFNEQIVSHFNLNDNNNNKVLSIPRDSLQFYNAVFSDDIFVTTNSEQIQNCVLNVPMYGPPTENNEYCEEISEKYPITPVSRFAYAKTKLKSTCAKASRKRLFNQLELSPPESFMEKKARSDENQLDGNKIKDDNQKLSSVGTFSVRPPYPPSSKDIRPEAPWLPEEDELLLLLLRRYSFNWEFVASRLTPPGLYIPLAEKRTAWDCFERWIQVDPRAANVQLTGSHARLAQQKLDESLRHSDKVSQHLSLRDEGTPNHLIKHNSYFLLPTVSRHYRPITIFEAIRKILKKREFAKKPTMTKRAIAPSAASTEKLPPVPSPLELSRLKSEREAQIQQIQAQRNFAQLQSQNRALRPQNAAVAAGAQQHNQQLAAFQAVAASQNSSNNSSAGVSPIAGRMVPRLQPYAVSSSLKLTPEQIHQLQQRKQTVPTTERTQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
137	Phosphorylation	EETPLKETSLELSEE CCCCCCCCCCCCCHH	36.70	21712547
138	Phosphorylation	ETPLKETSLELSEEE CCCCCCCCCCCCHHH	22.42	24763107
142	Phosphorylation	KETSLELSEEEIITS CCCCCCCCHHHHHHC	33.32	24763107
151	Phosphorylation	EEIITSKSPIPSPET HHHHHCCCCCCCHHH	28.03	24763107
155	Phosphorylation	TSKSPIPSPETIHKN HCCCCCCCHHHHCCC	35.77	25720772
170	Phosphorylation	IDVEEKETIEPTTPV CCHHHCCEECCCCCC	41.53	29996109
174	Phosphorylation	EKETIEPTTPVKEVE HCCEECCCCCCEEEE	30.83	29996109
175	Phosphorylation	KETIEPTTPVKEVET CCEECCCCCCEEEEE	36.48	29996109
183	Phosphorylation	PVKEVETTAHAEEEK CCEEEEECCCHHHHC	11.70	28889911
194	Phosphorylation	EEEKGPLTPDSEYAA HHHCCCCCCCHHHHH	28.34	28889911
197	Phosphorylation	KGPLTPDSEYAARQL CCCCCCCHHHHHHHH	33.44	21712547
212	Phosphorylation	TEELANKSSQEEGVD HHHHHHHHHHHCCHH	36.74	24763107
213	Phosphorylation	EELANKSSQEEGVDK HHHHHHHHHHCCHHH	43.13	25720772
298	Phosphorylation	DEVEEVHSPEAKVTE CCCEECCCCCCCCCC	29.61	28889911
342	Phosphorylation	IISVDKATESPVQEV EEECCCCCCCCCEEE	42.61	29996109
344	Phosphorylation	SVDKATESPVQEVAV ECCCCCCCCCEEEEE	26.47	28889911
375	Phosphorylation	QMENKLPSEKSPTID CCCCCCCCCCCCCCC	69.00	29996109
378	Phosphorylation	NKLPSEKSPTIDRTG CCCCCCCCCCCCCCC	24.19	28889911
380	Phosphorylation	LPSEKSPTIDRTGVE CCCCCCCCCCCCCCC	42.47	29996109
427	Phosphorylation	WLLRTEMSPLHLRLK HHHHCCCCCHHHHHC	20.34	28889911
823	Phosphorylation	NHLIKHNSYFLLPTV CCEEECCCEEECCCC	19.58	28889911
831	Phosphorylation	YFLLPTVSRHYRPIT EEECCCCCCCCCCCH	18.80	28889911

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 EAF_SCHPO !!

Functions of PTM Sites

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

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of EAF_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-298 AND SER-378, ANDMASS SPECTROMETRY.	18257517 [Abstract]