ELF1_SCHPO - dbPTM
ELF1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELF1_SCHPO
UniProt AC O14134
Protein Name mRNA export factor elf1
Gene Name elf1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1057
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Has a direct role in the mRNA export process. Appears to act within the rae1 mediated mRNA export pathway..
Protein Sequence MTSSVLIQGYEEDDVLKLLQELLDAETSQSCADVGKKIAQLFSNDNPLVTLKTTGFLDGLERAARNKKSGFHREAAMIGFATVIKNLGTPSEVVFLPYLPTILDSFSDRGEVVRQAAKMAAQALLDCLPAGAVETRLIPSLISYLDDSSIKWPSKVAALQLLGSLASSSPKAVADYMAALIPCIKERMHDTKPEISRAAITCMLNLCSVVENNDIIPHIPKLVDCMAHPETLEACIKDLSATTFVATVESVALAVLVPILKRALAQRSQSMLRLTVIITDNLCKLVPDPAEASDFLPELIPDVERIAQTAAMPEVRALASHALTTLNKAAAAQAAKAANNSEKQALDSACKELREAVLKNTSVPHELANSIIDYVCDALAALYKSNNFDKDKWTSQLGVLYLSPLVGEELASQISSKIYDDLHAFYKSLNSVDGISNLTIEEEELVNTDFSLAYGGRLLLSHTNLHLYRGHRYGVVGHNGCGKSTLLRAIGDYKVENFPSPDEVKTCFVAHSLQGEDTSMAILDFVAQDKALLTMNVTRQEAADALHSVGFTAEMQENPVASLSGGWKMKLELARAMLQKADILLLDEPTNHLDVANIAWLEAYLTSQKNITCLIVSHDSSFLDHVCTDIIHYEGVKNQAKKLGYYQGNLSAFVKVKPEAKSYYTLTATNEKFVFPPPGILTGVRSNTRLILKMTNASYTYPNAKKKSLDNVTVGLSLSSRVAILGPNGAGKSTLIKVLIGEVIPQEGKVFKHPNLRVGYVAQHAFHHLDQHLEKTPSQYIQWRYAGGQDREVSEKESRKLTEEDRAQLQRDITVNGERRRVEALIGRQKLKKSFQYEIKWFGKPHKYNTWVSREILLENGFQKFVQAFDDMESSREGLGFRELIPEDIRAHFEDVGLPGDIADYSPISSLSGGQKVKVVIAACLWNNPQLLVLDEPTNFLDRDALGGLAVAIRDWEGGVVMISHNEEFVSALCPEHWHVEAGKVTGKGKTAVDDGKFEDLSEKDLKKIEAKATKKKKLTRNEIKAKERRARERELAWLQSPKGTEKPKSFFSDDEE
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
2Phosphorylation------MTSSVLIQG
------CCCCEEECC
40.8029996109
3Phosphorylation-----MTSSVLIQGY
-----CCCCEEECCC
30.2429996109
4Phosphorylation----MTSSVLIQGYE
----CCCCEEECCCC
28.5129996109
663PhosphorylationVKPEAKSYYTLTATN
ECCCCCEEEEEEECC
10.3625720772
708PhosphorylationYPNAKKKSLDNVTVG
CCCCCCCCCCCEEEE
50.2429996109
713PhosphorylationKKSLDNVTVGLSLSS
CCCCCCEEEEEEHHC
18.3429996109
717PhosphorylationDNVTVGLSLSSRVAI
CCEEEEEEHHCCEEE
21.9229996109
733PhosphorylationGPNGAGKSTLIKVLI
CCCCCCHHHHHHHHH
27.7728889911
834PhosphorylationGRQKLKKSFQYEIKW
CHHHHHHHHCEEEEE
18.9225720772
1002PhosphorylationDGKFEDLSEKDLKKI
CCCCCCCCHHHHHHH
55.7224763107
1041PhosphorylationRELAWLQSPKGTEKP
HHHHHHHCCCCCCCC
26.8028889911
1050PhosphorylationKGTEKPKSFFSDDEE
CCCCCCCCCCCCCCC
39.8028889911
1053PhosphorylationEKPKSFFSDDEE---
CCCCCCCCCCCC---
41.9928889911

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 ELF1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELF1_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 ELF1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEX67_SCHPOmex67genetic
12110682
RAE1_SCHPOrae1genetic
12110682
SEM1_SCHPOrpn15genetic
15990877
NP106_SCHPOnpp106genetic
12110682
NU184_SCHPOnup184genetic
12110682

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELF1_SCHPO

loading...

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-733; SER-1041 ANDSER-1053, AND MASS SPECTROMETRY.

TOP