EFGM_YEAST - dbPTM
EFGM_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFGM_YEAST
UniProt AC P25039
Protein Name Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061}
Gene Name MEF1 {ECO:0000255|HAMAP-Rule:MF_03061}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 761
Subcellular Localization Mitochondrion .
Protein Description Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome..
Protein Sequence MSVQKMMWVPRKMVGGRIPFFTCSKVFSGFSRRSFHESPLARSTYEEEKVLVDEIKQKLTPDDIGRCNKLRNIGISAHIDSGKTTFTERVLYYTKRIKAIHEVRGRDNVGAKMDSMDLEREKGITIQSAATYCSWDKEGKNYHFNLIDTPGHIDFTIEVERALRVLDGAVLVVCAVSGVQSQTVTVDRQMRRYNVPRVTFINKMDRMGSDPFRAIEQLNSKLKIPAAAVQIPIGSESSLSGVVDLINRVAIYNKGDNGEIIEKGPVPENLKPLMEEKRQLLIETLADVDDEMAEMFLEEKEPTTQQIKDAIRRSTIARSFTPVLMGSALANTGIQPVLDAIVDYLPNPSEVLNTALDVSNNEAKVNLVPAVQQPFVGLAFKLEEGKYGQLTYVRVYQGRLRKGNYITNVKTGKKVKVARLVRMHSSEMEDVDEVGSGEICATFGIDCASGDTFTDGSVQYSMSSMYVPDAVVSLSITPNSKDASNFSKALNRFQKEDPTFRVKFDPESKETIISGMGELHLEIYVERMRREYNVDCVTGKPQVSYRESITIPADFDYTHKKQSGGAGQYGRVIGTLSPVDDITKGNIFETAIVGGRIPDKYLAACGKGFEEVCEKGPLIGHRVLDVKMLINDGAIHAVDSNELSFKTATMSAFRDAFLRAQPVIMEPIMNVSVTSPNEFQGNVIGLLNKLQAVIQDTENGHDEFTLKAECALSTMFGFATSLRASTQGKGEFSLEFSHYAPTAPHVQKELISEFQKKQAKK
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
24PhosphorylationRIPFFTCSKVFSGFS
CCCEEEECHHCCCCC		28.8828889911
28PhosphorylationFTCSKVFSGFSRRSF
EEECHHCCCCCCCCC		41.7524961812
31PhosphorylationSKVFSGFSRRSFHES
CHHCCCCCCCCCCCC		30.2424961812
34PhosphorylationFSGFSRRSFHESPLA
CCCCCCCCCCCCCCC		29.8222369663
38PhosphorylationSRRSFHESPLARSTY
CCCCCCCCCCCCCCC		19.3528889911
115PhosphorylationNVGAKMDSMDLEREK
CCCCCCCCCCCHHHH		15.6530377154
134PhosphorylationQSAATYCSWDKEGKN
EEEEEEECCCCCCCE		28.0928889911
203AcetylationPRVTFINKMDRMGSD
CCEEEECHHHHCCCC		37.0424489116
386AcetylationAFKLEEGKYGQLTYV
EEEECCCCCEEEEEE		49.8724489116
411PhosphorylationNYITNVKTGKKVKVA
CEEEECCCCCCEEEE		50.3728889911
550PhosphorylationVSYRESITIPADFDY
CEEEEEEEECCCCCC		30.1328889911
560AcetylationADFDYTHKKQSGGAG
CCCCCCCCCCCCCCC		44.7124489116
575PhosphorylationQYGRVIGTLSPVDDI
CCCCEEEEECCCCCC		16.9722369663
577PhosphorylationGRVIGTLSPVDDITK
CCEEEEECCCCCCCC		23.7922369663
583PhosphorylationLSPVDDITKGNIFET
ECCCCCCCCCCCEEE		39.6322369663
615AcetylationGFEEVCEKGPLIGHR
CHHHHHHHCCCCCCE		61.7824489116
756AcetylationELISEFQKKQAKK--
HHHHHHHHHHHCC--		52.7724489116
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 EFGM_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFGM_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 EFGM_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF5A1_YEASTHYP2physical
16554755
MNP1_YEASTMNP1physical
16554755
EIF3J_YEASTHCR1genetic
19061648
RS8A_YEASTRPS8Agenetic
19061648
RS8B_YEASTRPS8Agenetic
19061648
NMD5_YEASTNMD5genetic
19061648
LTV1_YEASTLTV1genetic
19061648
SSB1_YEASTSSB1physical
19536198
CDC15_YEASTCDC15genetic
27708008
PRS4_YEASTRPT2genetic
27708008
CDC13_YEASTCDC13genetic
27708008
CAB5_YEASTCAB5genetic
27708008
TSC11_YEASTTSC11genetic
27708008
ACT_YEASTACT1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
RCC1_YEASTSRM1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
TIM44_YEASTTIM44genetic
27708008
ARPC5_YEASTARC15genetic
27708008
HYM1_YEASTHYM1genetic
27708008
TAF4_YEASTTAF4genetic
27708008
DPOA_YEASTPOL1genetic
27708008
SYA_YEASTALA1genetic
27708008
SYLC_YEASTCDC60genetic
27708008
PSB5_YEASTPRE2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EFGM_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-34 AND SER-38, AND MASSSPECTROMETRY.

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