SEC62_SCHPO - dbPTM
SEC62_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEC62_SCHPO
UniProt AC O13787
Protein Name Translocation protein sec62
Gene Name sec62
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 273
Subcellular Localization Endoplasmic reticulum 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. In an initial step, the signal sequence seems to bind simultaneously to sec61 and sec62. sec62 and sec63 are required for interactions between sec61 and translocating polypeptides. sec62 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. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon (By similarity)..
Protein Sequence MDSSNVPVLKDEDKCKFSMRFTNFLKSRPELKTKPAILNGKRVYYFRVKRVLRFLTSEAYTPKKYKGFPEISSREEAIEVLKLLIMNSMLVRVDKLPPKQRKQKLVELQINRNQDFQDDMHYVWLYEPLPKRVMALAVLFALVVLALVLFPLWPMFMRKGAWYLSMGGLGVIGLFFVLVILRFFLFCITAVIVRPGIWLFPNLLADVGFCDSFKPLWSWHNSKSEVKKTRKSKKLSKKATSPAASATPEKSSTSTTSLKNLRHRNPTVEEVSE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
240PhosphorylationKKLSKKATSPAASAT
HHHHHHCCCCCCCCC
44.0925720772
241PhosphorylationKLSKKATSPAASATP
HHHHHCCCCCCCCCC
19.8724763107
245PhosphorylationKATSPAASATPEKSS
HCCCCCCCCCCCCCC
34.4829996109
247PhosphorylationTSPAASATPEKSSTS
CCCCCCCCCCCCCCC
29.5025720772
251PhosphorylationASATPEKSSTSTTSL
CCCCCCCCCCCCCCH
36.8729996109
253PhosphorylationATPEKSSTSTTSLKN
CCCCCCCCCCCCHHH
36.8625720772
254PhosphorylationTPEKSSTSTTSLKNL
CCCCCCCCCCCHHHH
31.4729996109
255PhosphorylationPEKSSTSTTSLKNLR
CCCCCCCCCCHHHHH
22.0929996109
256PhosphorylationEKSSTSTTSLKNLRH
CCCCCCCCCHHHHHH
31.6529996109
257PhosphorylationKSSTSTTSLKNLRHR
CCCCCCCCHHHHHHC
37.1229996109
267PhosphorylationNLRHRNPTVEEVSE-
HHHHCCCCHHHHCC-
44.0621712547
272PhosphorylationNPTVEEVSE------
CCCHHHHCC------
40.6519547744

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 SEC62_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEC62_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 SEC62_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAD1_SCHPOsad1physical
23695164
SWS1_SCHPOsws1physical
26771498
SAD1_SCHPOsad1physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEC62_SCHPO

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Related Literatures of Post-Translational Modification

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