dbPTM

ETFB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ETFB_HUMAN
UniProt AC	P38117
Protein Name	Electron transfer flavoprotein subunit beta {ECO:0000305}
Gene Name	ETFB {ECO:0000312\|HGNC:HGNC:3482}
Organism	Homo sapiens (Human).
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. [PubMed: 25416781]
Protein Sequence	MAELRVLVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCEIAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGADRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLGKQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVEREIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKKKKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTEDLVAKLKEIGRI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 2)	Phosphorylation	-	25.24	20068231
2	Acetylation	------MAELRVLVA ------CCHHHHHHH	25.24	25944712
4 (in isoform 2)	Phosphorylation	-	3.13	20068231
8 (in isoform 2)	Phosphorylation	-	5.42	20068231
11	Acetylation	LRVLVAVKRVIDYAV HHHHHHHHHHHHEEE	31.07	25953088
11	Ubiquitination	LRVLVAVKRVIDYAV HHHHHHHHHHHHEEE	31.07	33845483
11 (in isoform 2)	Phosphorylation	-	31.07	20068231
17 (in isoform 2)	Phosphorylation	-	7.74	20860994
19	2-Hydroxyisobutyrylation	RVIDYAVKIRVKPDR HHHHEEEEEEECCCC	19.34	-
19	Ubiquitination	RVIDYAVKIRVKPDR HHHHEEEEEEECCCC	19.34	33845483
19	Acetylation	RVIDYAVKIRVKPDR HHHHEEEEEEECCCC	19.34	25953088
26	Methylation	KIRVKPDRTGVVTDG EEEECCCCCCEECCC	41.74	-
35	Ubiquitination	GVVTDGVKHSMNPFC CEECCCCCCCCCCCH	35.18	29967540
35	Acetylation	GVVTDGVKHSMNPFC CEECCCCCCCCCCCH	35.18	26051181
37	Phosphorylation	VTDGVKHSMNPFCEI ECCCCCCCCCCCHHH	17.97	26126808
42	Glutathionylation	KHSMNPFCEIAVEEA CCCCCCCHHHHHHHH	3.79	22555962
56	Acetylation	AVRLKEKKLVKEVIA HHHHHHHHCCCEEEE	60.65	26051181
59	2-Hydroxyisobutyrylation	LKEKKLVKEVIAVSC HHHHHCCCEEEECCC	57.61	-
59	Malonylation	LKEKKLVKEVIAVSC HHHHHCCCEEEECCC	57.61	26320211
59	Acetylation	LKEKKLVKEVIAVSC HHHHHCCCEEEECCC	57.61	26051181
65	Phosphorylation	VKEVIAVSCGPAQCQ CCEEEECCCCHHHHH	12.34	23403867
65	O-linked_Glycosylation	VKEVIAVSCGPAQCQ CCEEEECCCCHHHHH	12.34	31373491
74	Phosphorylation	GPAQCQETIRTALAM CHHHHHHHHHHHHHH	7.00	23403867
77	Phosphorylation	QCQETIRTALAMGAD HHHHHHHHHHHHCCC	23.36	23403867
85	Methylation	ALAMGADRGIHVEVP HHHHCCCCCEEEECC	45.49	-
110	Ubiquitination	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	33845483
110	Succinylation	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	23954790
110	Acetylation	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	23236377
110	2-Hydroxyisobutyrylation	QVARVLAKLAEKEKV HHHHHHHHHHHHHCC	44.03	-
114	Acetylation	VLAKLAEKEKVDLVL HHHHHHHHHCCCEEE	58.17	25953088
114	Ubiquitination	VLAKLAEKEKVDLVL HHHHHHHHHCCCEEE	58.17	-
116	Succinylation	AKLAEKEKVDLVLLG HHHHHHHCCCEEEEC	52.71	23954790
116	Acetylation	AKLAEKEKVDLVLLG HHHHHHHCCCEEEEC	52.71	23236377
116	Ubiquitination	AKLAEKEKVDLVLLG HHHHHHHCCCEEEEC	52.71	29967540
116	2-Hydroxyisobutyrylation	AKLAEKEKVDLVLLG HHHHHHHCCCEEEEC	52.71	-
126	Ubiquitination	LVLLGKQAIDDDCNQ EEEECCCCCCCCCCC	15.63	29967540
154	Phosphorylation	GTFASQVTLEGDKLK CCEEEEEEEECCEEE	16.08	28176443
172	Phosphorylation	EIDGGLETLRLKLPA EECCCCEEEEEECCE	23.40	-
176	Ubiquitination	GLETLRLKLPAVVTA CCEEEEEECCEEEEE	46.09	29967540
176	2-Hydroxyisobutyrylation	GLETLRLKLPAVVTA CCEEEEEECCEEEEE	46.09	-
182	Phosphorylation	LKLPAVVTADLRLNE EECCEEEEEECCCCC	14.09	-
186	Methylation	AVVTADLRLNEPRYA EEEEEECCCCCCCHH	35.69	-
192	Phosphorylation	LRLNEPRYATLPNIM CCCCCCCHHCCCHHH	18.04	28796482
194	Phosphorylation	LNEPRYATLPNIMKA CCCCCHHCCCHHHHH	33.54	27499020
200	Acetylation	ATLPNIMKAKKKKIE HCCCHHHHHHHCCEE	53.94	30588593
200	Succinylation	ATLPNIMKAKKKKIE HCCCHHHHHHHCCEE	53.94	23954790
200	"N6,N6,N6-trimethyllysine"	ATLPNIMKAKKKKIE HCCCHHHHHHHCCEE	53.94	-
200	Methylation	ATLPNIMKAKKKKIE HCCCHHHHHHHCCEE	53.94	24129315
201	Ubiquitination	TLPNIMKAKKKKIEV CCCHHHHHHHCCEEE	16.12	33845483
202	Ubiquitination	LPNIMKAKKKKIEVI CCHHHHHHHCCEEEE	60.65	-
202	Methylation	LPNIMKAKKKKIEVI CCHHHHHHHCCEEEE	60.65	24129315
202	"N6,N6-dimethyllysine"	LPNIMKAKKKKIEVI CCHHHHHHHCCEEEE	60.65	-
203	"N6,N6,N6-trimethyllysine"	PNIMKAKKKKIEVIK CHHHHHHHCCEEEEC	65.25	-
203	Methylation	PNIMKAKKKKIEVIK CHHHHHHHCCEEEEC	65.25	25023281
205	2-Hydroxyisobutyrylation	IMKAKKKKIEVIKPG HHHHHHCCEEEECCC	53.64	-
205	Malonylation	IMKAKKKKIEVIKPG HHHHHHCCEEEECCC	53.64	26320211
207	Ubiquitination	KAKKKKIEVIKPGDL HHHHCCEEEECCCCC	47.25	29967540
210	Succinylation	KKKIEVIKPGDLGVD HCCEEEECCCCCCCC	48.39	-
210	Ubiquitination	KKKIEVIKPGDLGVD HCCEEEECCCCCCCC	48.39	-
210	Malonylation	KKKIEVIKPGDLGVD HCCEEEECCCCCCCC	48.39	26320211
210	Succinylation	KKKIEVIKPGDLGVD HCCEEEECCCCCCCC	48.39	27452117
210	Acetylation	KKKIEVIKPGDLGVD HCCEEEECCCCCCCC	48.39	20167786
219	Phosphorylation	GDLGVDLTSKLSVIS CCCCCCCCCCEEEEE	21.25	20068231
220	Phosphorylation	DLGVDLTSKLSVISV CCCCCCCCCEEEEEC	38.61	20068231
221	Acetylation	LGVDLTSKLSVISVE CCCCCCCCEEEEECC	39.28	30588599
223	Phosphorylation	VDLTSKLSVISVEDP CCCCCCEEEEECCCC	22.57	21712546
226	Phosphorylation	TSKLSVISVEDPPQR CCCEEEEECCCCCCC	19.80	20166139
234	Phosphorylation	VEDPPQRTAGVKVET CCCCCCCCCCCEEEC	23.63	24719451
238	Acetylation	PQRTAGVKVETTEDL CCCCCCCEEECHHHH	33.17	26051181
248	Acetylation	TTEDLVAKLKEIGRI CHHHHHHHHHHHCCC	53.24	23954790
248	Succinylation	TTEDLVAKLKEIGRI CHHHHHHHHHHHCCC	53.24	-
248	Malonylation	TTEDLVAKLKEIGRI CHHHHHHHHHHHCCC	53.24	26320211
248	2-Hydroxyisobutyrylation	TTEDLVAKLKEIGRI CHHHHHHHHHHHCCC	53.24	-
248	Succinylation	TTEDLVAKLKEIGRI CHHHHHHHHHHHCCC	53.24	-
248	Ubiquitination	TTEDLVAKLKEIGRI CHHHHHHHHHHHCCC	53.24	29967540
250	Ubiquitination	EDLVAKLKEIGRI-- HHHHHHHHHHCCC--	46.72	-
267	Ubiquitination	------------------- -------------------		29967540
339	Ubiquitination	------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------		29967540

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 ETFB_HUMAN !!

Functions of PTM Sites

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

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 ETFB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
ETFA_HUMAN	ETFA	physical	26344197
GPX4_HUMAN	GPX4	physical	26344197
PIPNB_HUMAN	PITPNB	physical	26344197
GMCL1_HUMAN	GMCL1	physical	28514442
AKA11_HUMAN	AKAP11	physical	28514442
KNL1_HUMAN	CASC5	physical	28514442
DSN1_HUMAN	DSN1	physical	28514442
PLCH1_HUMAN	PLCH1	physical	28514442
KAP1_HUMAN	PRKAR1B	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
231680	Glutaric aciduria 2B (GA2B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ETFB_HUMAN

Related Literatures of Post-Translational Modification

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