dbPTM

SC232_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SC232_SCHPO
UniProt AC	O94672
Protein Name	Protein transport protein sec23-2
Gene Name	sec232
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	765
Subcellular Localization	Cytoplasm . Cytoplasmic vesicle, COPII-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side. Golgi apparatus membrane Peripheral membrane protein Cytoplasmi
Protein Description	Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity)..
Protein Sequence	MNFEDIEDQDGIRLSWNTFSATPAENARAVIPIAAMYTPLHENERMTIEQYDPVACRAPCRAVLNPYCHVDLRARFWICPFCFQRNPLPAQYSDISSNSLPLELLSQSTTMEYVLSKPVKSPPVFLFVMDTAVDESELTALKDAVIVSLSLLPPDAIVGLITYGSLIQVHEIGFEAMPKSYVFQPAADYSTMKLQQLLALSGNQIRSSSSKAKISGTGITLNLGAASRFLMPVQKCEMHLLNILEQLQPDCLEVPAGQRQLRCTGAAVKIASDLLGIAFPKCGSRIELFCGGPCTVGLGQVVSTELKEPMRSHSEIANDKAKHFKKSKKFYSSLAERLSNQGHALDLFAGCLDQVGIMEMENLVNNTGGAIVLSDSFTTSIFKQSFQRLFSVDASGYLKMGFMANLEVLTSKGLTICGMIGNGVGENKKGTNISDTQIGISKTNSWKMAAISPKSSYALYFDLGKEMGNPNSQRPTQAFIQFLTYYQHSSGTYRLRVTTISRSFITGNAKSISESFDQEAAAAIVARMALFKCQTEDEMSVTRWIDRNLIRLCQHFADYRKEDPSSFRLLPNFTLYPQFIFHLRRSPFLHIFNNSPDETSFYRHMLNVADVNDSLIMIQPTLQSYSFNEPEGVPVLLDSVSIKPDVILLLDTYFHILIFHGSTIAQWRNAGYQEQPEYVNLKELLLAPRLEVTELLADRFPIPRFIVCDQGGSQARFLLSRINPSVSFNKSSQFSPMSKDSETVLTDDVNLQKFMDHLRKMAVIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
209	Phosphorylation	GNQIRSSSSKAKISG CCCCCCCCCCCEECC	36.78	27738172
210	Phosphorylation	NQIRSSSSKAKISGT CCCCCCCCCCEECCC	38.28	24763107
565	Phosphorylation	DYRKEDPSSFRLLPN HHCCCCCCCCCCCCC	55.20	28889911
566	Phosphorylation	YRKEDPSSFRLLPNF HCCCCCCCCCCCCCC	21.55	28889911
735	Phosphorylation	FNKSSQFSPMSKDSE CCCCCCCCCCCCCCC	16.44	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 SC232_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SC232_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 SC232_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SC232_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of SC232_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-565 AND SER-566, ANDMASS SPECTROMETRY.	18257517 [Abstract]