DED1_SCHPO - dbPTM
DED1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DED1_SCHPO
UniProt AC O13370
Protein Name ATP-dependent RNA helicase ded1
Gene Name ded1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 636
Subcellular Localization Cytoplasm .
Protein Description ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Inactivation of ded1 blocks mitotic cell cycle progression at G1 and G2/M. Induces sexual development and ascus formation..
Protein Sequence MSDNVQQQVDSVGSVTEKLQKTNISRPRKYIPPFARDKPSAGAAPAVGDDESVSSRGSSRSQTPSEFSSNYGGRREYNRGGHYGGGEGRQNNYRGGREGGYSNGGGYRNNRGFGQWRDGQHVIGARNTLLERQLFGAVADGTKVSTGINFEKYDDIPVEVSGGDIEPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAVPVDQDAGMGYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKVVHVEDSEKRSYLLDILHTLPPEGLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIELLQEANQECPSFLIAMARESSFGGNGRGGRYSGRGGRGGNAYGARDFRRPTNSSSGYSSGPSYSGYGGFESRTPHHGNTYNSGSAQSWW
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------MSDNVQQQV
------CCHHHHHHH		37.5821712547
11PhosphorylationNVQQQVDSVGSVTEK
HHHHHHHHHHHHHHH		29.5324763107
14PhosphorylationQQVDSVGSVTEKLQK
HHHHHHHHHHHHHHH		24.5824763107
40PhosphorylationPFARDKPSAGAAPAV
CCCCCCCCCCCCCCC		45.1125720772
52PhosphorylationPAVGDDESVSSRGSS
CCCCCCCCCCCCCCC		34.0028889911
54PhosphorylationVGDDESVSSRGSSRS
CCCCCCCCCCCCCCC		24.4828889911
55PhosphorylationGDDESVSSRGSSRSQ
CCCCCCCCCCCCCCC		38.2128889911
58PhosphorylationESVSSRGSSRSQTPS
CCCCCCCCCCCCCCC		22.8228889911
59PhosphorylationSVSSRGSSRSQTPSE
CCCCCCCCCCCCCCH		38.4828889911
61PhosphorylationSSRGSSRSQTPSEFS
CCCCCCCCCCCCHHH		40.1129996109
63PhosphorylationRGSSRSQTPSEFSSN
CCCCCCCCCCHHHCC		29.9928889911
65PhosphorylationSSRSQTPSEFSSNYG
CCCCCCCCHHHCCCC		55.4525720772
68PhosphorylationSQTPSEFSSNYGGRR
CCCCCHHHCCCCCCC		17.3929996109
69PhosphorylationQTPSEFSSNYGGRRE
CCCCHHHCCCCCCCC		39.1225720772
102PhosphorylationGGREGGYSNGGGYRN
CCCCCCCCCCCCCCC		32.0725720772
128PhosphorylationHVIGARNTLLERQLF
EEECCCCCHHHHHHH		27.4528889911
173PhosphorylationEPVNEFTSPPLNSHL
CCCCCCCCCCCCHHH		29.8229996109
312PhosphorylationGCDLLSATPGRLVDL
CCCCCCCCCCCHHHH		23.9328889911
399PhosphorylationLSVGRVGSTSENITQ
EEECCCCCCCCCEEE		26.3828889911
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 DED1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DED1_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 DED1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CG22_SCHPOcig2genetic
10725227
CG22_SCHPOcig2genetic
23322785
RL32A_SCHPOrpl3202physical
19682301
RL8_SCHPOrpl8physical
19682301
RL18A_SCHPOrpl1801physical
19682301
RL27B_SCHPOrpl2702physical
19682301
RL29_SCHPOrpl29physical
19682301
RS13_SCHPOrps13physical
19682301
LYS1_SCHPOlys3physical
19682301
GBLP_SCHPOcpc2physical
19682301
DDX3X_HUMANDDX3Xgenetic
25724843
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DED1_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-52; SER-54; SER-55;SER-58; SER-59; THR-63; THR-128 AND THR-312, AND MASS SPECTROMETRY.

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