dbPTM

SEC63_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SEC63_SCHPO
UniProt AC	Q9HGN7
Protein Name	Translocation protein sec63
Gene Name	sec63
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	611
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein . Nucleus membrane Multi-pass membrane protein. Nucleus inner membrane Multi-pass membrane protein.
Protein Description	Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon. sec63 may affect sec61-polypeptide interactions by increasing the affinity of targeting pathways for sec61 and/or by modifying sec61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation (By similarity)..
Protein Sequence	MSSEYKYDEQGIFFPVFLLVGTSCCVLPLTYSTILGPSASKEKKNVRDPFQKYRPKDLKVQRKSIFRLRYIFLILGWLAIGFLSYKIANSRLKLNIWDPYEILGIAKGTSVDDVRRHYKRLSIKFHPDKVRNMVNTTREEVEKHYIEITNAYRALTDDKTRENYALYGTPDVPQHISVGIALPKWISESENSIYILGFYGLVFGIVLPYAVGKWWYGSRTYTRDHVHVDTVDEWFPKMETSLTLDELLSLFASSKELTSLVPNEKNPKEYILKLLFDHLNRKKTNNFNTHQILSQSDVVLNALLSVATAFGFANPVDNVLKLWQHIVQAIPLDAPFPLLQLPHLLMEDVKNLSIRNISSIPQFLSLSEEQTKDYLPNYSKNQLKEMREIANGIPRISVVAAKVLVDDDEYITVGAIANLILDLKCSYGTEVVPEVSTDGTETATKKDEEDAEKYHQSKDVVLGDVETLPYAWAPYFTQHHKTAWWIYVVDPRQNRVIVPPFSITDIPKTLRTFRIPFQVPPVAGTFSFQLHIMSNSYVGEDVISNLTMIVKDTSVLQEQLQEEAVSDLEDNSDIDESANAGKDFSDDENIGSDEEDESEYDPMDTDTSDGE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
566	Phosphorylation	QLQEEAVSDLEDNSD HHHHHHHHHCCCCCC	43.45	28889911
572	Phosphorylation	VSDLEDNSDIDESAN HHHCCCCCCHHHHHH	48.54	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 SEC63_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SEC63_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 SEC63_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SEC63_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of SEC63_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-566 AND SER-572, ANDMASS SPECTROMETRY.	18257517 [Abstract]