dbPTM

YF3E_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YF3E_SCHPO
UniProt AC	O13905
Protein Name	BSD domain-containing protein C22A12.14c
Gene Name	SPAC22A12.14c
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	347
Subcellular Localization	Cytoplasm .
Protein Description
Protein Sequence	MDLYDYMAPTTTTEEDDEEGYEKLKEEMGSALNNLTNGKFGLFWNSMKEKSENFLDDTKGKASSGMQQLKSQLEENIPVNSAMENLRKVEETAGSFWSGFGSTVNGFLDQALQISPKEDDVSTPTHEASSSVFLNRHERQLLELVQNENTFTQIISEPSHGITFESWEKEISIDGKTEEISLLLEEYPDLRKQMESLVPSEVSYDDFWKRFFWHKEVVQPIKAIQSGNDEEEIFSWGDERSDEEESDNEQVNDEKKQSSEEDTTENNSAAEVIDETVNDLESAVSKGLQIETQPASHDGEVDGEVKEEEENKVSSSSNIEASQSSLEVKDEANRKVDDDDEDDDDWE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
122	Phosphorylation	SPKEDDVSTPTHEAS CCCCCCCCCCCCHHC	35.35	25720772
123	Phosphorylation	PKEDDVSTPTHEASS CCCCCCCCCCCHHCH	31.86	28889911
125	Phosphorylation	EDDVSTPTHEASSSV CCCCCCCCCHHCHHH	32.22	28889911
129	Phosphorylation	STPTHEASSSVFLNR CCCCCHHCHHHHCCH	21.84	25720772
130	Phosphorylation	TPTHEASSSVFLNRH CCCCHHCHHHHCCHH	37.25	25720772
131	Phosphorylation	PTHEASSSVFLNRHE CCCHHCHHHHCCHHH	17.88	25720772
235	Phosphorylation	NDEEEIFSWGDERSD CCHHHHCCCCCCCCC	35.49	28889911
241	Phosphorylation	FSWGDERSDEEESDN CCCCCCCCCCCCCCC	47.53	28889911
246	Phosphorylation	ERSDEEESDNEQVND CCCCCCCCCCCCCCH	49.36	28889911
258	Phosphorylation	VNDEKKQSSEEDTTE CCHHHHHCCCCCCCC	48.90	24763107
259	Phosphorylation	NDEKKQSSEEDTTEN CHHHHHCCCCCCCCC	42.38	24763107
263	Phosphorylation	KQSSEEDTTENNSAA HHCCCCCCCCCCHHH	39.01	29996109
264	Phosphorylation	QSSEEDTTENNSAAE HCCCCCCCCCCHHHH	49.38	29996109
268	Phosphorylation	EDTTENNSAAEVIDE CCCCCCCHHHHHHHH	40.20	29996109
292	Phosphorylation	SKGLQIETQPASHDG HCCCEEEEECCCCCC	41.29	21712547
296	Phosphorylation	QIETQPASHDGEVDG EEEEECCCCCCCCCC	28.88	28889911
322	Phosphorylation	SSSNIEASQSSLEVK CCCCCCHHHCHHHCC	20.15	24763107
324	Phosphorylation	SNIEASQSSLEVKDE CCCCHHHCHHHCCHH	34.10	24763107
325	Phosphorylation	NIEASQSSLEVKDEA CCCHHHCHHHCCHHH	22.40	24763107

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 YF3E_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YF3E_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 YF3E_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of YF3E_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of YF3E_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 THR-123; THR-125; SER-235;SER-241 AND SER-246, AND MASS SPECTROMETRY.	18257517 [Abstract]