ETFB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ETFB_MOUSE
• UniProt AC: Q9DCW4
• Protein Name: Electron transfer flavoprotein subunit beta {ECO:0000305}
• Gene Name: Etfb {ECO:0000312|MGI:MGI:106098}
• Organism: Mus musculus (Mouse).
• Sequence Length: 255
• Subcellular Localization: Mitochondrion matrix .
• Protein Description: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (By similarity). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. [PubMed: 25023281 ETFB binds an AMP molecule that probably has a purely structural role (By similarity]
• Protein Sequence: MAELRALVAVKRVIDFAVKIRVKPDKSGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEIIAVSCGPSQCQETIRTALAMGADRGIHVEIPGAQAESLGPLQVARVLAKLAEKEKVDLLFLGKQAIDDDCNQTGQMTAGLLDWPQGTFASQVTLEGDKVKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVVKAGDLGVDLTSKVSVISVEEPPQRSAGVKVETTEDLVAKLKEVGRI

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
2	Acetylation	------MAELRALVA ------CHHHHHHHH	25.24	-
19	Acetylation	RVIDFAVKIRVKPDK HHHEEEEEEEECCCC	22.74	23806337
19	Succinylation	RVIDFAVKIRVKPDK HHHEEEEEEEECCCC	22.74	23806337
23	Acetylation	FAVKIRVKPDKSGVV EEEEEEECCCCCCCC	37.34	2395229
26	Acetylation	KIRVKPDKSGVVTDG EEEECCCCCCCCCCC	58.60	23864654
35	Acetylation	GVVTDGVKHSMNPFC CCCCCCCCCCCCCHH	35.18	23864654
35	Succinylation	GVVTDGVKHSMNPFC CCCCCCCCCCCCCHH	35.18	23806337
42	S-nitrosocysteine	KHSMNPFCEIAVEEA CCCCCCHHHHHHHHH	3.79	-
42	Glutathionylation	KHSMNPFCEIAVEEA CCCCCCHHHHHHHHH	3.79	24333276
42	S-nitrosylation	KHSMNPFCEIAVEEA CCCCCCHHHHHHHHH	3.79	22178444
42	S-palmitoylation	KHSMNPFCEIAVEEA CCCCCCHHHHHHHHH	3.79	26165157
56	Succinylation	AVRLKEKKLVKEIIA HHHHHHHHCCCEEEE	60.65	26388266
56	Acetylation	AVRLKEKKLVKEIIA HHHHHHHHCCCEEEE	60.65	24062335
59	Glutarylation	LKEKKLVKEIIAVSC HHHHHCCCEEEECCC	54.34	24703693
59	Acetylation	LKEKKLVKEIIAVSC HHHHHCCCEEEECCC	54.34	23864654
59	Succinylation	LKEKKLVKEIIAVSC HHHHHCCCEEEECCC	54.34	23806337
65	Phosphorylation	VKEIIAVSCGPSQCQ CCEEEECCCCHHHHH	12.34	29472430
69	Phosphorylation	IAVSCGPSQCQETIR EECCCCHHHHHHHHH	28.95	25521595
74	Phosphorylation	GPSQCQETIRTALAM CHHHHHHHHHHHHHH	7.00	29472430
77	Phosphorylation	QCQETIRTALAMGAD HHHHHHHHHHHHCCC	23.36	22817900
98	Phosphorylation	IPGAQAESLGPLQVA CCCCCCHHCCHHHHH	41.46	22817900
110	Malonylation	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	26320211
110	Acetylation	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	23864654
110	Succinylation	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	23806337
110	Glutarylation	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	24703693
114	Succinylation	VLAKLAEKEKVDLLF HHHHHHHHHCCEEEE	58.17	26388266
114	Acetylation	VLAKLAEKEKVDLLF HHHHHHHHHCCEEEE	58.17	24062335
116	Ubiquitination	AKLAEKEKVDLLFLG HHHHHHHCCEEEEEC	52.71	-
116	Succinylation	AKLAEKEKVDLLFLG HHHHHHHCCEEEEEC	52.71	23806337
116	Acetylation	AKLAEKEKVDLLFLG HHHHHHHCCEEEEEC	52.71	23864654
124	Acetylation	VDLLFLGKQAIDDDC CEEEEECCHHCCCCC	38.41	23864654
131	S-nitrosylation	KQAIDDDCNQTGQMT CHHCCCCCCCCCCCC	5.38	21278135
131	S-nitrosocysteine	KQAIDDDCNQTGQMT CHHCCCCCCCCCCCC	5.38	-
134	Phosphorylation	IDDDCNQTGQMTAGL CCCCCCCCCCCCCCC	18.52	23140645
138	Phosphorylation	CNQTGQMTAGLLDWP CCCCCCCCCCCCCCC	15.08	23140645
148	Phosphorylation	LLDWPQGTFASQVTL CCCCCCCCEEEEEEE	15.69	23140645
151	Phosphorylation	WPQGTFASQVTLEGD CCCCCEEEEEEEECC	22.46	23140645
176	Ubiquitination	GLETLRLKLPAVVTA CCEEEEEECCEEEEE	46.09	-
176	Acetylation	GLETLRLKLPAVVTA CCEEEEEECCEEEEE	46.09	23864654
176	Glutarylation	GLETLRLKLPAVVTA CCEEEEEECCEEEEE	46.09	24703693
182	Phosphorylation	LKLPAVVTADLRLNE EECCEEEEEECCCCC	14.09	-
194	Phosphorylation	LNEPRYATLPNIMKA CCCCCHHCCCHHHHH	33.54	-
200	Methylation	ATLPNIMKAKKKKIE HCCCHHHHHCCCCEE	53.94	25023281
200	"N6,N6,N6-trimethyllysine"	ATLPNIMKAKKKKIE HCCCHHHHHCCCCEE	53.94	-
200	Acetylation	ATLPNIMKAKKKKIE HCCCHHHHHCCCCEE	53.94	23576753
202	Acetylation	LPNIMKAKKKKIEVV CCHHHHHCCCCEEEE	60.65	23576753
203	Methylation	PNIMKAKKKKIEVVK CHHHHHCCCCEEEEE	65.25	25023281
203	"N6,N6,N6-trimethyllysine"	PNIMKAKKKKIEVVK CHHHHHCCCCEEEEE	65.25	-
203	Acetylation	PNIMKAKKKKIEVVK CHHHHHCCCCEEEEE	65.25	23576753
204	Acetylation	NIMKAKKKKIEVVKA HHHHHCCCCEEEEEC	59.27	23576753
205	Succinylation	IMKAKKKKIEVVKAG HHHHCCCCEEEEECC	53.64	24315375
205	Acetylation	IMKAKKKKIEVVKAG HHHHCCCCEEEEECC	53.64	24062335
210	Ubiquitination	KKKIEVVKAGDLGVD CCCEEEEECCCCCCC	52.40	-
210	Acetylation	KKKIEVVKAGDLGVD CCCEEEEECCCCCCC	52.40	23576753
210	Malonylation	KKKIEVVKAGDLGVD CCCEEEEECCCCCCC	52.40	26320211
210	Succinylation	KKKIEVVKAGDLGVD CCCEEEEECCCCCCC	52.40	23806337
210	Succinylation	KKKIEVVKAGDLGVD CCCEEEEECCCCCCC	52.40	-
219	Phosphorylation	GDLGVDLTSKVSVIS CCCCCCCCCCEEEEE	23.26	-
221	Acetylation	LGVDLTSKVSVISVE CCCCCCCCEEEEECC	33.04	23864654
223	Phosphorylation	VDLTSKVSVISVEEP CCCCCCEEEEECCCC	19.92	-
226	Phosphorylation	TSKVSVISVEEPPQR CCCEEEEECCCCCCC	22.71	30352176
234	Phosphorylation	VEEPPQRSAGVKVET CCCCCCCCCCCEEEE	24.91	22817900
238	Ubiquitination	PQRSAGVKVETTEDL CCCCCCCEEEEHHHH	33.17	-
238	Succinylation	PQRSAGVKVETTEDL CCCCCCCEEEEHHHH	33.17	23806337
238	Acetylation	PQRSAGVKVETTEDL CCCCCCCEEEEHHHH	33.17	23576753
242	Phosphorylation	AGVKVETTEDLVAKL CCCEEEEHHHHHHHH	17.62	22817900
248	Ubiquitination	TTEDLVAKLKEVGRI EHHHHHHHHHHHCCC	53.24	-
248	Glutarylation	TTEDLVAKLKEVGRI EHHHHHHHHHHHCCC	53.24	24703693
248	Succinylation	TTEDLVAKLKEVGRI EHHHHHHHHHHHCCC	53.24	23806337
248	Acetylation	TTEDLVAKLKEVGRI EHHHHHHHHHHHCCC	53.24	23576753
248	Succinylation	TTEDLVAKLKEVGRI EHHHHHHHHHHHCCC	53.24	-
250	Acetylation	EDLVAKLKEVGRI-- HHHHHHHHHHCCC--	50.04	23576753

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
200	K	Methylation	Trimethylation at Lys-200 and Lys-203 may negatively regulate the activity in electron transfer from acyl-CoA dehydrogenases.	23576753
203	K	Methylation	Trimethylation at Lys-200 and Lys-203 may negatively regulate the activity in electron transfer from acyl-CoA dehydrogenases.	25023281

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of ETFB_MOUSE !!

Drug and Disease Associations

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