ECM32_YEAST - dbPTM
ECM32_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECM32_YEAST
UniProt AC P32644
Protein Name Putative ATP-dependent RNA helicase ECM32
Gene Name ECM32
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1121
Subcellular Localization Cytoplasm . Associated with polyribosomes.
Protein Description Probable RNA helicase, which may be involved in modulation of the translation termination process. Probably unwinds double-stranded RNA. In vitro, unwinds covalently closed, circular DNA in the presence of a DNA topoisomerase TOP1 and replication factor-A protein RFA1..
Protein Sequence MDFQCRTCSQAYDAEQMMKHLSSTRHKTVFDTSNDEDICCEECQDKNIHQLQIIRFGGEDMVLLCNSCFRKEYSETERPSTSYSLQNGSILKFWEKYVKVRECCCDECGEESNLNANRNGEVLCDKCLPKSNRAKDFVSEKSGRFLYIYLGLNETQNSTRKPRKKGGRRVGRGKKGRKGAKIKKEKKETFEAKISRIAYEVKKENSTIQSSSSSNLRNFKGFKAVESDPVVAAKVSKSETSRSNPGPSNRNKGKGNKANHKKNSGNGIGKEKERKTNIRNNVRNSQPIPEDRKNTNSHVTTNSGGKGKNESVDKHQLPQPKALNGNGSGSTNTTGLKKGKKDHAGQKTKGNDKTGNKNPREAKLNSAGRKNALGKKSNNQPNKGTSRWTIGSDTESSREPSISPNENTTSITKSRNRNKKASKPTLNEKSKTTTMPKKLETKNQEKNNGKTKDGKLIYEEGEPLTRYNTFKSTLSYPDLNTYLNDYSFALFLEQKLENEFVQNFNILWPRNEKDTAFIINVEKNNNSELEKLLPANLLALGRPAFNERQPFFFCTQDEQKVWYIFIKELSIQRGKYVLLVELFSWNNLSLPTKNGSSQFKLLPTSAQTSRILFAMTRITNPKFIDLLLGQKPIKEIYFDNRLKFSSDKLNRSQKTAVEHVLNNSITILQGPPGTGKTSTIEEIIIQVIERFHAFPILCVAASNIAIDNIAEKIMENRPQIKILRILSKKKEQQYSDDHPLGEICLHNIVYKNLSPDMQVVANKTRRGEMISKSEDTKFYKEKNRVTNKVVSQSQIIFTTNIAAGGRELKVIKECPVVIMDEATQSSEASTLVPLSLPGIRNFVFVGDEKQLSSFSNIPQLETSLFERVLSNGTYKNPLMLDTQYRMHPKISEFPIKKIYNGELKDGVTDEQKAWPGVQHPLFFYQCDLGPESRVRSTQRDIVGFTYENKHECVEIVKIIQILMLDKKVPLEEIGVITPYSAQRDLLSDILTKNVVINPKQISMQQEYDEIELFNAAGSQGTAGSLQNNVINIINGLHVATVDSFQGHEKSFIIFSCVRNNTENKIGFLRDKRRLNVALTRAKHGLIVVGNKNVLRKGDPLWKDYITYLEEQEVIFTDLTAY
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
96AcetylationSILKFWEKYVKVREC
CHHHHHHHHCHHHHH		46.0324489116
97PhosphorylationILKFWEKYVKVRECC
HHHHHHHHCHHHHHC		8.2521126336
112PhosphorylationCDECGEESNLNANRN
CCCCCCCCCCCCCCC		42.1728889911
206PhosphorylationYEVKKENSTIQSSSS
HHHHHHCCCCCCCCC		28.1622369663
207PhosphorylationEVKKENSTIQSSSSS
HHHHHCCCCCCCCCC		34.3222369663
210PhosphorylationKENSTIQSSSSSNLR
HHCCCCCCCCCCCCC		28.4722369663
211PhosphorylationENSTIQSSSSSNLRN
HCCCCCCCCCCCCCC		20.1925521595
212PhosphorylationNSTIQSSSSSNLRNF
CCCCCCCCCCCCCCC		42.9322369663
213PhosphorylationSTIQSSSSSNLRNFK
CCCCCCCCCCCCCCC		25.7820377248
214PhosphorylationTIQSSSSSNLRNFKG
CCCCCCCCCCCCCCC		41.6620377248
223AcetylationLRNFKGFKAVESDPV
CCCCCCEEEECCCCE		61.2625381059
227PhosphorylationKGFKAVESDPVVAAK
CCEEEECCCCEEEEE		40.3925752575
243PhosphorylationSKSETSRSNPGPSNR
CCCCCCCCCCCCCCC		47.3328889911
311PhosphorylationGGKGKNESVDKHQLP
CCCCCCCCCCHHCCC		45.0430377154
385PhosphorylationNNQPNKGTSRWTIGS
CCCCCCCCCCEEECC		19.4124961812
386PhosphorylationNQPNKGTSRWTIGSD
CCCCCCCCCEEECCC		34.1924961812
389PhosphorylationNKGTSRWTIGSDTES
CCCCCCEEECCCCCC		17.8522369663
392PhosphorylationTSRWTIGSDTESSRE
CCCEEECCCCCCCCC		37.1922369663
394PhosphorylationRWTIGSDTESSREPS
CEEECCCCCCCCCCC		39.1922369663
396PhosphorylationTIGSDTESSREPSIS
EECCCCCCCCCCCCC		36.4720377248
397PhosphorylationIGSDTESSREPSISP
ECCCCCCCCCCCCCC		34.1422369663
401PhosphorylationTESSREPSISPNENT
CCCCCCCCCCCCCCC		30.8321440633
403PhosphorylationSSREPSISPNENTTS
CCCCCCCCCCCCCCC		26.4723749301
430PhosphorylationKPTLNEKSKTTTMPK
CCCCCHHHCCCCCCH		29.1128889911
465PhosphorylationYEEGEPLTRYNTFKS
EECCCCCCCCCCCCC		41.6520377248
467PhosphorylationEGEPLTRYNTFKSTL
CCCCCCCCCCCCCCC		17.2023749301
469PhosphorylationEPLTRYNTFKSTLSY
CCCCCCCCCCCCCCC		24.4120377248
597PhosphorylationLPTKNGSSQFKLLPT
CCCCCCCCCCEECCC		40.8227017623
604PhosphorylationSQFKLLPTSAQTSRI
CCCEECCCCHHHHHH		36.3427017623
608PhosphorylationLLPTSAQTSRILFAM
ECCCCHHHHHHHHHH		21.4927017623
622AcetylationMTRITNPKFIDLLLG
HHHCCCHHHHHHHCC		57.9524489116
772AcetylationRRGEMISKSEDTKFY
CCCCCCCCCCCCCHH		47.1125381059
932PhosphorylationQCDLGPESRVRSTQR
ECCCCCHHHCCCCCC		38.9325704821
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 ECM32_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECM32_YEAST !!
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 ECM32_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS104_YEASTHSP104genetic
10836794
PFD6_YEASTYKE2genetic
19061648
SYMM_YEASTMSM1genetic
19061648
MED8_YEASTMED8genetic
27708008
NOP14_YEASTNOP14genetic
27708008
HEM6_YEASTHEM13genetic
27708008
SLU7_YEASTSLU7genetic
27708008
TAF12_YEASTTAF12genetic
27708008
GPI19_YEASTGPI19genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SAD1_YEASTSAD1genetic
27708008
ZPR1_YEASTZPR1genetic
27708008
YHS2_YEASTCIA2genetic
27708008
NU192_YEASTNUP192genetic
27708008
PRP19_YEASTPRP19genetic
27708008
BOS1_YEASTBOS1genetic
27708008
CDC42_YEASTCDC42genetic
27708008
SEC22_YEASTSEC22genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECM32_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; SER-227;SER-392; THR-465 AND THR-469, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND MASSSPECTROMETRY.

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