EFTU_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EFTU_RAT
• UniProt AC: P85834
• Protein Name: Elongation factor Tu, mitochondrial
• Gene Name: Tufm {ECO:0000250|UniProtKB:P49411}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 452
• Subcellular Localization: Mitochondrion .
• Protein Description: Plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIG-I/DDX58-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy. Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis..
• Protein Sequence: MAAATLLRATPRFSGLCASPTPFLQGRLRPLKAPASPFLCRGLAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLEKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDVPAMTEEDKNIKWS

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
79	Acetylation	TLTAAITKILAEGGG HHHHHHHHHHHCCCC	29.61	22902405
88	Acetylation	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	22902405
88	Succinylation	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	-
90	Acetylation	EGGGAKFKKYEEIDN CCCCCCCCCHHHCCC	54.46	22902405
91	Succinylation	GGGAKFKKYEEIDNA CCCCCCCCHHHCCCC	62.11	26843850
91	Acetylation	GGGAKFKKYEEIDNA CCCCCCCCHHHCCCC	62.11	22902405
234	Succinylation	RDPELGVKSVQKLLD CCHHHCHHHHHHHHH	43.01	-
238	Acetylation	LGVKSVQKLLDAVDT HCHHHHHHHHHHHHH	49.19	22902405
256	Acetylation	VPTRDLEKPFLLPVE CCCCCCCCCCEEEEE	48.65	22902405
264	Phosphorylation	PFLLPVESVYSIPGR CCEEEEEEEEECCCC	26.96	23991683
266	Phosphorylation	LLPVESVYSIPGRGT EEEEEEEEECCCCCE	15.34	23991683
267	Phosphorylation	LPVESVYSIPGRGTV EEEEEEEECCCCCEE	21.83	23991683
278	Phosphorylation	RGTVVTGTLERGILK CCEEEEEEEECCEEC	18.97	-
286	Succinylation	LERGILKKGDECELL EECCEECCCCEEEEC	69.05	26843850
304	Phosphorylation	KNIRTVVTGIEMFHK CCCHHHHHHHHHHHH	28.27	25575281
312	Phosphorylation	GIEMFHKSLERAEAG HHHHHHHHHHHHHCC	27.22	23991683
342	Acetylation	RRGLVMVKPGSIQPH HCCEEEECCCCCCCC	26.09	22902405
361	Acetylation	AQVYILSKEEGGRHK EEEEEEECCCCCCCC	57.23	22902405
405	Acetylation	AMPGEDLKLSLILRQ CCCCCHHCHHHHCCC	48.64	22902405
407	O-linked_Glycosylation	PGEDLKLSLILRQPM CCCHHCHHHHCCCCE	16.27	27213235
418	Acetylation	RQPMILEKGQRFTLR CCCEEECCCCCEEEC	57.82	22902405
430	Phosphorylation	TLRDGNKTIGTGLVT EECCCCEEECCCEEE	28.74	28689409
447	Acetylation	PAMTEEDKNIKWS-- CCCCHHHCCCCCC--	64.94	22902405

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EFTU_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EFTU_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EFTU_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of EFTU_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.