ELOH1_SCHPO - dbPTM
ELOH1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELOH1_SCHPO
UniProt AC Q9UTF7
Protein Name Putative elongation of fatty acids protein 1 {ECO:0000250|UniProtKB:P40319}
Gene Name SPAC1B2.03c {ECO:0000312|PomBase:SPAC1B2.03c}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 334
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description May be involved in the synthesis of very long chain fatty acids..
Protein Sequence MDLTGAHMLKIHRPSIDHPFGVDLWHLFEQLSIKTIGWNPSEFEYIPGKTPMSQWSSVIVSITAYYVIILSGRAIMTNRKPLKQRRLFQLHNFILTIISGALLALLVEEVFRNYMRNGLFYCVCDSRHFTQRLVTLYYLNYLTKYLELMDTVFLFLKKKPLAFLHCYHHGITALLCFTQLLGRTSVQWGVIGLNLYVHVIMYSYYFLAACGRRVWWKQWVTRVQIIQFVLDLILCYFGTYSHIAFRYFPWLPHVGDCSGSLFAAFFGCGVLSSYLFLFIGFYINTYIKRGAKKNQRKAAGKADNTSVAAAAGSEALAATTATNASPFSARSRKL
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
319PhosphorylationGSEALAATTATNASP
CCHHHHHHCCCCCCC
16.0321712547
320PhosphorylationSEALAATTATNASPF
CHHHHHHCCCCCCCC
27.1021712547
322PhosphorylationALAATTATNASPFSA
HHHHHCCCCCCCCCC
29.2621712547
325PhosphorylationATTATNASPFSARSR
HHCCCCCCCCCCCCC
28.6628889911
328PhosphorylationATNASPFSARSRKL-
CCCCCCCCCCCCCC-
26.5921712547
331PhosphorylationASPFSARSRKL----
CCCCCCCCCCC----
33.2221712547

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 ELOH1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELOH1_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 ELOH1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ELOH1_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELOH1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-325, AND MASSSPECTROMETRY.

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