EFTS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EFTS_HUMAN
• UniProt AC: P43897
• Protein Name: Elongation factor Ts, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03135}
• Gene Name: TSFM {ECO:0000255|HAMAP-Rule:MF_03135}
• Organism: Homo sapiens (Human).
• Sequence Length: 325
• Subcellular Localization: Mitochondrion.
• Protein Description: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome..
• Protein Sequence: MSLLRSLRVFLVARTGSYPAGSLLRQSPQPRHTFYAGPRLSASASSKELLMKLRRKTGYSFVNCKKALETCGGDLKQAEIWLHKEAQKEGWSKAAKLQGRKTKEGLIGLLQEGNTTVLVEVNCETDFVSRNLKFQLLVQQVALGTMMHCQTLKDQPSAYSKGFLNSSELSGLPAGPDREGSLKDQLALAIGKLGENMILKRAAWVKVPSGFYVGSYVHGAMQSPSLHKLVLGKYGALVICETSEQKTNLEDVGRRLGQHVVGMAPLSVGSLDDEPGGEAETKMLSQPYLLDPSITLGQYVQPQGVSVVDFVRFECGEGEEAAETE

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
22	Phosphorylation	TGSYPAGSLLRQSPQ CCCCCCCHHHCCCCC	26.74	-
33	Phosphorylation	QSPQPRHTFYAGPRL CCCCCCCEEECCCCC	21.44	24719451
35	Phosphorylation	PQPRHTFYAGPRLSA CCCCCEEECCCCCCC	16.29	24719451
41	Phosphorylation	FYAGPRLSASASSKE EECCCCCCCCCCCHH	22.81	26552605
43	Phosphorylation	AGPRLSASASSKELL CCCCCCCCCCCHHHH	25.88	26552605
45	Phosphorylation	PRLSASASSKELLMK CCCCCCCCCHHHHHH	39.17	26552605
46	Phosphorylation	RLSASASSKELLMKL CCCCCCCCHHHHHHH	29.84	26552605
52	Malonylation	SSKELLMKLRRKTGY CCHHHHHHHHHHHCC	38.52	26320211
52	Acetylation	SSKELLMKLRRKTGY CCHHHHHHHHHHHCC	38.52	27452117
56	Malonylation	LLMKLRRKTGYSFVN HHHHHHHHHCCCEEC	39.61	26320211
56	Succinylation	LLMKLRRKTGYSFVN HHHHHHHHHCCCEEC	39.61	27452117
59	Phosphorylation	KLRRKTGYSFVNCKK HHHHHHCCCEECHHH	12.27	-
65	Succinylation	GYSFVNCKKALETCG CCCEECHHHHHHHCC	35.56	23954790
65	Acetylation	GYSFVNCKKALETCG CCCEECHHHHHHHCC	35.56	25953088
66	Ubiquitination	YSFVNCKKALETCGG CCEECHHHHHHHCCC	61.48	-
71	S-nitrosylation	CKKALETCGGDLKQA HHHHHHHCCCCHHHH	4.13	19483679
71	S-nitrosocysteine	CKKALETCGGDLKQA HHHHHHHCCCCHHHH	4.13	-
76	Succinylation	ETCGGDLKQAEIWLH HHCCCCHHHHHHHHH	52.80	-
76	Acetylation	ETCGGDLKQAEIWLH HHCCCCHHHHHHHHH	52.80	25953088
76	Succinylation	ETCGGDLKQAEIWLH HHCCCCHHHHHHHHH	52.80	-
76	Malonylation	ETCGGDLKQAEIWLH HHCCCCHHHHHHHHH	52.80	26320211
84	Ubiquitination	QAEIWLHKEAQKEGW HHHHHHHHHHHHHCH	53.20	-
84	Acetylation	QAEIWLHKEAQKEGW HHHHHHHHHHHHHCH	53.20	26051181
133	Succinylation	DFVSRNLKFQLLVQQ CCCCCHHHHHHHHHH	34.31	-
133	Succinylation	DFVSRNLKFQLLVQQ CCCCCHHHHHHHHHH	34.31	-
160	Phosphorylation	KDQPSAYSKGFLNSS CCCCCHHHCCCCCHH	26.47	23401153
161 (in isoform 1)	Ubiquitination	-	40.79	21890473
161	Ubiquitination	DQPSAYSKGFLNSSE CCCCHHHCCCCCHHH	40.79	21906983
183	Ubiquitination	PDREGSLKDQLALAI CCCCCCHHHHHHHHH	45.16	-
192	Succinylation	QLALAIGKLGENMIL HHHHHHHHHCCCHHE	47.40	2189047
192	Ubiquitination	QLALAIGKLGENMIL HHHHHHHHHCCCHHE	47.40	21890473
192 (in isoform 1)	Ubiquitination	-	47.40	21890473
192	Acetylation	QLALAIGKLGENMIL HHHHHHHHHCCCHHE	47.40	23236377
192	Succinylation	QLALAIGKLGENMIL HHHHHHHHHCCCHHE	47.40	-
192	Ubiquitination	QLALAIGKLGENMIL HHHHHHHHHCCCHHE	47.40	-
200	Ubiquitination	LGENMILKRAAWVKV HCCCHHEEEEEEEEC	29.12	-
212	Phosphorylation	VKVPSGFYVGSYVHG EECCCCCCCCHHHCC	13.87	17053785
213 (in isoform 2)	Ubiquitination	-	3.71	21890473
216	Phosphorylation	SGFYVGSYVHGAMQS CCCCCCHHHCCCCCC	7.19	17053785
223	Phosphorylation	YVHGAMQSPSLHKLV HHCCCCCCCCHHHHH	11.90	-
240	S-nitrosylation	KYGALVICETSEQKT CCCEEEEECCCCCCC	3.48	19483679
240	S-nitrosocysteine	KYGALVICETSEQKT CCCEEEEECCCCCCC	3.48	-
246	Ubiquitination	ICETSEQKTNLEDVG EECCCCCCCCHHHHH	35.02	-
263	Sulfoxidation	LGQHVVGMAPLSVGS HHHCCEEECCCCCCC	2.04	21406390
267	Phosphorylation	VVGMAPLSVGSLDDE CEEECCCCCCCCCCC	24.31	28450419
270	Phosphorylation	MAPLSVGSLDDEPGG ECCCCCCCCCCCCCC	26.86	25159151
281	Phosphorylation	EPGGEAETKMLSQPY CCCCCCCHHCCCCCE	28.89	28450419
291 (in isoform 2)	Phosphorylation	-	32.10	27251275
324	Phosphorylation	EGEEAAETE------ CCHHHHCCC------	42.12	25159151
345 (in isoform 2)	Phosphorylation	-		24719451

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RRFM_HUMAN	MRRF	physical	22939629
AT7L2_HUMAN	ATXN7L2	physical	28514442
IF2M_HUMAN	MTIF2	physical	28514442
CYTT_HUMAN	CST2	physical	28514442
CYTS_HUMAN	CST4	physical	28514442
ZG16B_HUMAN	ZG16B	physical	28514442
TRUA_HUMAN	PUS1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 610505: Combined oxidative phosphorylation deficiency 3 (COXPD3)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-212 AND TYR-216, ANDMASS SPECTROMETRY.
PubMed: 17053785