EFTU_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EFTU_MOUSE
• UniProt AC: Q8BFR5
• Protein Name: Elongation factor Tu, mitochondrial
• Gene Name: Tufm
• Organism: Mus musculus (Mouse).
• Sequence Length: 452
• Subcellular Localization: Mitochondrion .
• Protein Description: Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays also 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..
• Protein Sequence: MAAATLLRATPRFSGLCASPTPFLQGRLRPLKAPASPFLCRGLAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLAKQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEQRDPELGVKSVQKLLDAVDTYIPVPTRDLDKPFLLPVESVYSIPGRGTVVTGTLERGILKKGDECELLGHNKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIQPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRVILPPGKELAMPGEDLKLSLILRQPMILEKGQRFTLRDGNKTIGTGLVTDVPAMTEEDKNIKWS

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
55	Acetylation	KKTYVRDKPHVNVGT ECCEECCCCCEEEEE	26.85	23864654
71	Phosphorylation	GHVDHGKTTLTAAIT EEECCCHHHHHHHHH	31.46	28576409
72	Phosphorylation	HVDHGKTTLTAAITK EECCCHHHHHHHHHH	26.12	28576409
74	Phosphorylation	DHGKTTLTAAITKIL CCCHHHHHHHHHHHH	16.38	28576409
78	Phosphorylation	TTLTAAITKILAEGG HHHHHHHHHHHHCCC	13.80	28576409
79	Ubiquitination	TLTAAITKILAEGGG HHHHHHHHHHHCCCC	29.61	-
79	Acetylation	TLTAAITKILAEGGG HHHHHHHHHHHCCCC	29.61	23576753
79	Succinylation	TLTAAITKILAEGGG HHHHHHHHHHHCCCC	29.61	24315375
88	Glutarylation	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	24703693
88	Succinylation	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	23806337
88	Acetylation	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	23806337
88	Ubiquitination	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	-
90	Acetylation	EGGGAKFKKYEEIDN CCCCCCCCCHHHCCC	54.46	23201123
91	Acetylation	GGGAKFKKYEEIDNA CCCCCCCCHHHCCCC	62.11	23201123
91	Glutarylation	GGGAKFKKYEEIDNA CCCCCCCCHHHCCCC	62.11	24703693
127	S-nitrosylation	RHYAHTDCPGHADYV HHCCCCCCCCCHHHH	4.58	21278135
127	Glutathionylation	RHYAHTDCPGHADYV HHCCCCCCCCCHHHH	4.58	24333276
127	S-nitrosocysteine	RHYAHTDCPGHADYV HHCCCCCCCCCHHHH	4.58	-
147	S-nitrosylation	GTAPLDGCILVVAAN CCCCCCCEEEEEEEC	1.86	21278135
147	S-nitrosocysteine	GTAPLDGCILVVAAN CCCCCCCEEEEEEEC	1.86	-
222	S-nitrosocysteine	VIVGSALCALEQRDP EEEECHHHHHHHCCH	3.98	-
222	Glutathionylation	VIVGSALCALEQRDP EEEECHHHHHHHCCH	3.98	24333276
222	S-palmitoylation	VIVGSALCALEQRDP EEEECHHHHHHHCCH	3.98	28526873
222	S-nitrosylation	VIVGSALCALEQRDP EEEECHHHHHHHCCH	3.98	21278135
234	Acetylation	RDPELGVKSVQKLLD CCHHHCHHHHHHHHH	43.01	23806337
234	Succinylation	RDPELGVKSVQKLLD CCHHHCHHHHHHHHH	43.01	23806337
234	Malonylation	RDPELGVKSVQKLLD CCHHHCHHHHHHHHH	43.01	26320211
238	Acetylation	LGVKSVQKLLDAVDT HCHHHHHHHHHHHHH	49.19	23576753
256	Succinylation	VPTRDLDKPFLLPVE CCCCCCCCCCEEECC	44.99	23954790
256	Acetylation	VPTRDLDKPFLLPVE CCCCCCCCCCEEECC	44.99	23806337
264	Phosphorylation	PFLLPVESVYSIPGR CCEEECCEEEECCCC	26.96	29472430
266	Phosphorylation	LLPVESVYSIPGRGT EEECCEEEECCCCCE	15.34	29472430
267	Phosphorylation	LPVESVYSIPGRGTV EECCEEEECCCCCEE	21.83	29472430
273	Phosphorylation	YSIPGRGTVVTGTLE EECCCCCEEEEEEEE	15.50	22817900
276	Phosphorylation	PGRGTVVTGTLERGI CCCCEEEEEEEECCE	21.80	19854140
278	Phosphorylation	RGTVVTGTLERGILK CCEEEEEEEECCEEC	18.97	-
286	Acetylation	LERGILKKGDECELL EECCEECCCCEEEEC	69.05	23806337
286	Succinylation	LERGILKKGDECELL EECCEECCCCEEEEC	69.05	23806337
290	S-nitrosylation	ILKKGDECELLGHNK EECCCCEEEECCCCC	5.48	21278135
290	Glutathionylation	ILKKGDECELLGHNK EECCCCEEEECCCCC	5.48	24333276
290	S-nitrosocysteine	ILKKGDECELLGHNK EECCCCEEEECCCCC	5.48	-
297	Acetylation	CELLGHNKNIRTVVT EEECCCCCCCHHHHH	48.34	23864654
312	Phosphorylation	GIEMFHKSLERAEAG HHHHHHHHHHHHHCC	27.22	21082442
342	Acetylation	RRGLVMVKPGSIQPH HCCEEEECCCCCCCC	26.09	24062335
351	Acetylation	GSIQPHQKVEAQVYI CCCCCCCEEEEEEEE	38.72	23954790
361	Acetylation	AQVYILSKEEGGRHK EEEEEEECCCCCCCC	57.23	23576753
361	Succinylation	AQVYILSKEEGGRHK EEEEEEECCCCCCCC	57.23	26388266
405	Acetylation	AMPGEDLKLSLILRQ CCCCCHHCHHHHCCC	48.64	23954790
418	Acetylation	RQPMILEKGQRFTLR CCCEEECCCCCEEEC	57.82	23954790
447	Acetylation	PAMTEEDKNIKWS-- CCCCHHHCCCCCC--	64.94	23806337

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

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

Functions of PTM Sites

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

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EFTU_MOUSE !!

Drug and Disease Associations

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