EFGM_HUMAN - dbPTM
EFGM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFGM_HUMAN
UniProt AC Q96RP9
Protein Name Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061}
Gene Name GFM1 {ECO:0000255|HAMAP-Rule:MF_03061}
Organism Homo sapiens (Human).
Sequence Length 751
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. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis..
Protein Sequence MRLLGAAAVAALGRGRAPASLGWQRKQVNWKACRWSSSGVIPNEKIRNIGISAHIDSGKTTLTERVLYYTGRIAKMHEVKGKDGVGAVMDSMELERQRGITIQSAATYTMWKDVNINIIDTPGHVDFTIEVERALRVLDGAVLVLCAVGGVQCQTMTVNRQMKRYNVPFLTFINKLDRMGSNPARALQQMRSKLNHNAAFMQIPMGLEGNFKGIVDLIEERAIYFDGDFGQIVRYGEIPAELRAAATDHRQELIECVANSDEQLGEMFLEEKIPSISDLKLAIRRATLKRSFTPVFLGSALKNKGVQPLLDAVLEYLPNPSEVQNYAILNKEDDSKEKTKILMNSSRDNSHPFVGLAFKLEVGRFGQLTYVRSYQGELKKGDTIYNTRTRKKVRLQRLARMHADMMEDVEEVYAGDICALFGIDCASGDTFTDKANSGLSMESIHVPDPVISIAMKPSNKNDLEKFSKGIGRFTREDPTFKVYFDTENKETVISGMGELHLEIYAQRLEREYGCPCITGKPKVAFRETITAPVPFDFTHKKQSGGAGQYGKVIGVLEPLDPEDYTKLEFSDETFGSNIPKQFVPAVEKGFLDACEKGPLSGHKLSGLRFVLQDGAHHMVDSNEISFIRAGEGALKQALANATLCILEPIMAVEVVAPNEFQGQVIAGINRRHGVITGQDGVEDYFTLYADVPLNDMFGYSTELRSCTEGKGEYTMEYSRYQPCLPSTQEDVINKYLEATGQLPVKKGKAKN
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
14MethylationAAVAALGRGRAPASL
HHHHHHCCCCCCHHH		32.07-
592-HydroxyisobutyrylationSAHIDSGKTTLTERV
EEEECCCCCCHHHHH		42.14-
68PhosphorylationTLTERVLYYTGRIAK
CHHHHHHHHHHCCEE		8.9819835603
69PhosphorylationLTERVLYYTGRIAKM
HHHHHHHHHHCCEEC		9.8819835603
82UbiquitinationKMHEVKGKDGVGAVM
ECEEECCCCCCCHHH		45.66-
82 (in isoform 2)Ubiquitination-45.66-
89SulfoxidationKDGVGAVMDSMELER
CCCCCHHHCHHHHHH		2.9021406390
91PhosphorylationGVGAVMDSMELERQR
CCCHHHCHHHHHHHH		8.9623911959
121PhosphorylationVNINIIDTPGHVDFT
EEEEEECCCCCCCEE		22.29-
128PhosphorylationTPGHVDFTIEVERAL
CCCCCCEEEEHHHHH		16.27-
165PhosphorylationVNRQMKRYNVPFLTF
CCHHHHHCCCCHHHH		18.2620860994
175AcetylationPFLTFINKLDRMGSN
CHHHHHHHHHHCCCC		47.1219608861
224PhosphorylationLIEERAIYFDGDFGQ
HHHHCEEEECCCCCC		8.47-
249 (in isoform 2)Phosphorylation-29.0325599653
275PhosphorylationFLEEKIPSISDLKLA
HHHCCCCCHHHHHHH		37.8929396449
277PhosphorylationEEKIPSISDLKLAIR
HCCCCCHHHHHHHHH		41.0324275569
280 (in isoform 1)Ubiquitination-40.6421890473
280UbiquitinationIPSISDLKLAIRRAT
CCCHHHHHHHHHHHH		40.6421906983
291PhosphorylationRRATLKRSFTPVFLG
HHHHHHHHCCCEECH		31.7021712546
293PhosphorylationATLKRSFTPVFLGSA
HHHHHHCCCEECHHH		21.57-
299 (in isoform 2)Ubiquitination-32.3521890473
321 (in isoform 2)Ubiquitination-57.97-
323 (in isoform 2)Ubiquitination-5.40-
340MalonylationDDSKEKTKILMNSSR
CCCHHHHEEEECCCC		44.9326320211
345PhosphorylationKTKILMNSSRDNSHP
HHEEEECCCCCCCCC		16.88-
359 (in isoform 2)Malonylation-37.8226320211
372MethylationFGQLTYVRSYQGELK
CCEEEEEEEECCEEC		21.16-
3792-HydroxyisobutyrylationRSYQGELKKGDTIYN
EEECCEECCCCEEEC		50.86-
380UbiquitinationSYQGELKKGDTIYNT
EECCEECCCCEEECC		74.72-
385PhosphorylationLKKGDTIYNTRTRKK
ECCCCEEECCCCHHH		16.7529496907
458PhosphorylationISIAMKPSNKNDLEK
EEEEECCCCHHHHHH		55.7230576142
467PhosphorylationKNDLEKFSKGIGRFT
HHHHHHHHHHCCCCC		40.8330576142
468MalonylationNDLEKFSKGIGRFTR
HHHHHHHHHCCCCCC		58.6526320211
468AcetylationNDLEKFSKGIGRFTR
HHHHHHHHHCCCCCC		58.6518603139
487 (in isoform 2)Malonylation-69.0526320211
520AcetylationGCPCITGKPKVAFRE
CCCCCCCCCEEEEEE		32.7727452117
540AcetylationVPFDFTHKKQSGGAG
CCCCCCCCCCCCCCC		49.8325953088
540SuccinylationVPFDFTHKKQSGGAG
CCCCCCCCCCCCCCC		49.8327452117
551UbiquitinationGGAGQYGKVIGVLEP
CCCCCCCEEEEEEEC		26.24-
564PhosphorylationEPLDPEDYTKLEFSD
ECCCHHHCCCCEECC		12.24-
565PhosphorylationPLDPEDYTKLEFSDE
CCCHHHCCCCEECCC		41.28-
566UbiquitinationLDPEDYTKLEFSDET
CCHHHCCCCEECCCC		39.53-
580UbiquitinationTFGSNIPKQFVPAVE
CCCCCCCHHHHHHHH		53.20-
605PhosphorylationPLSGHKLSGLRFVLQ
CCCCCCCCCCEEEEE		40.3524719451
710AcetylationLRSCTEGKGEYTMEY
EECCCCCCCEEEEEE		42.1926051181
713PhosphorylationCTEGKGEYTMEYSRY
CCCCCCEEEEEECCC		21.7624043423
714PhosphorylationTEGKGEYTMEYSRYQ
CCCCCEEEEEECCCC		10.1424043423
717PhosphorylationKGEYTMEYSRYQPCL
CCEEEEEECCCCCCC		6.3924043423
718PhosphorylationGEYTMEYSRYQPCLP
CEEEEEECCCCCCCC		15.9424043423
735PhosphorylationQEDVINKYLEATGQL
HHHHHHHHHHHHCCC		12.8021406692
739PhosphorylationINKYLEATGQLPVKK
HHHHHHHHCCCCCCC		18.9821406692
7452-HydroxyisobutyrylationATGQLPVKKGKAKN-
HHCCCCCCCCCCCC-		54.60-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFGM_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL23A_HUMANRPL23Aphysical
26344197
EFTU_HUMANTUFMphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609060Combined oxidative phosphorylation deficiency 1 (COXPD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EFGM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175, AND MASS SPECTROMETRY.

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