dbPTM

ETFA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ETFA_HUMAN
UniProt AC	P13804
Protein Name	Electron transfer flavoprotein subunit alpha, mitochondrial
Gene Name	ETFA
Organism	Homo sapiens (Human).
Sequence Length	333
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: 27499296]
Protein Sequence	MFRAAAPGQLRRAASLLRFQSTLVIAEHANDSLAPITLNTITAATRLGGEVSCLVAGTKCDKVAQDLCKVAGIAKVLVAQHDVYKGLLPEELTPLILATQKQFNYTHICAGASAFGKNLLPRVAAKLEVAPISDIIAIKSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFDAAATSGGSASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLFKVVPEMTEILKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	GQLRRAASLLRFQST HHHHHHHHHHHHHCE	27.27	28674151
32	Phosphorylation	IAEHANDSLAPITLN EEECCCCCCCCCHHH	26.66	-
36	Ubiquitination	ANDSLAPITLNTITA CCCCCCCCHHHHHHH	5.94	21890473
37	Phosphorylation	NDSLAPITLNTITAA CCCCCCCHHHHHHHH	16.94	-
42	Phosphorylation	PITLNTITAATRLGG CCHHHHHHHHHHCCC	14.27	22817900
45	Phosphorylation	LNTITAATRLGGEVS HHHHHHHHHCCCEEE	24.78	-
52	Phosphorylation	TRLGGEVSCLVAGTK HHCCCEEEEEECCCC	9.46	21712546
53	S-nitrosocysteine	RLGGEVSCLVAGTKC HCCCEEEEEECCCCC	4.24	-
53	S-nitrosylation	RLGGEVSCLVAGTKC HCCCEEEEEECCCCC	4.24	19483679
59	2-Hydroxyisobutyrylation	SCLVAGTKCDKVAQD EEEECCCCCHHHHHH	39.25	-
59	Acetylation	SCLVAGTKCDKVAQD EEEECCCCCHHHHHH	39.25	25953088
59	Malonylation	SCLVAGTKCDKVAQD EEEECCCCCHHHHHH	39.25	26320211
59	Succinylation	SCLVAGTKCDKVAQD EEEECCCCCHHHHHH	39.25	-
59	Succinylation	SCLVAGTKCDKVAQD EEEECCCCCHHHHHH	39.25	-
62	2-Hydroxyisobutyrylation	VAGTKCDKVAQDLCK ECCCCCHHHHHHHHH	49.27	-
62	Acetylation	VAGTKCDKVAQDLCK ECCCCCHHHHHHHHH	49.27	25953088
62	Ubiquitination	VAGTKCDKVAQDLCK ECCCCCHHHHHHHHH	49.27	-
69	Acetylation	KVAQDLCKVAGIAKV HHHHHHHHHHHHHHH	42.28	25825284
69	Malonylation	KVAQDLCKVAGIAKV HHHHHHHHHHHHHHH	42.28	26320211
69	Succinylation	KVAQDLCKVAGIAKV HHHHHHHHHHHHHHH	42.28	-
69	Succinylation	KVAQDLCKVAGIAKV HHHHHHHHHHHHHHH	42.28	27452117
69	Ubiquitination	KVAQDLCKVAGIAKV HHHHHHHHHHHHHHH	42.28	-
75	Acetylation	CKVAGIAKVLVAQHD HHHHHHHHHHHHCCC	33.89	26051181
75	Ubiquitination	CKVAGIAKVLVAQHD HHHHHHHHHHHHCCC	33.89	-
84	Phosphorylation	LVAQHDVYKGLLPEE HHHCCCHHHCCCCHH	12.85	-
85	Acetylation	VAQHDVYKGLLPEEL HHCCCHHHCCCCHHH	42.82	23954790
85	Succinylation	VAQHDVYKGLLPEEL HHCCCHHHCCCCHHH	42.82	-
85	Succinylation	VAQHDVYKGLLPEEL HHCCCHHHCCCCHHH	42.82	21890473
85	Ubiquitination	VAQHDVYKGLLPEEL HHCCCHHHCCCCHHH	42.82	21890473
85	Ubiquitination	VAQHDVYKGLLPEEL HHCCCHHHCCCCHHH	42.82	21890473
90	Ubiquitination	VYKGLLPEELTPLIL HHHCCCCHHHHHHHH	66.66	21890473
93	Phosphorylation	GLLPEELTPLILATQ CCCCHHHHHHHHHCC	21.23	25850435
101	Acetylation	PLILATQKQFNYTHI HHHHHCCCCCCCCCC	53.13	25038526
126	Ubiquitination	LLPRVAAKLEVAPIS HHHHHHHHCEEEEHH	35.13	21890473
133	Phosphorylation	KLEVAPISDIIAIKS HCEEEEHHHEEEECC	23.00	22199227
139	2-Hydroxyisobutyrylation	ISDIIAIKSPDTFVR HHHEEEECCCCCCEE	47.08	-
139	Acetylation	ISDIIAIKSPDTFVR HHHEEEECCCCCCEE	47.08	23236377
139	Succinylation	ISDIIAIKSPDTFVR HHHEEEECCCCCCEE	47.08	23954790
139	Ubiquitination	ISDIIAIKSPDTFVR HHHEEEECCCCCCEE	47.08	21890473
139	Ubiquitination	ISDIIAIKSPDTFVR HHHEEEECCCCCCEE	47.08	21890473
140	Phosphorylation	SDIIAIKSPDTFVRT HHEEEECCCCCCEEE	23.15	29255136
143	Phosphorylation	IAIKSPDTFVRTIYA EEECCCCCCEEEEEC	27.67	22199227
147	Phosphorylation	SPDTFVRTIYAGNAL CCCCCEEEEECCCEE	17.03	26074081
149	Phosphorylation	DTFVRTIYAGNALCT CCCEEEEECCCEEEE	14.08	28152594
156	Phosphorylation	YAGNALCTVKCDEKV ECCCEEEEEECCCCE	24.69	26074081
158	Acetylation	GNALCTVKCDEKVKV CCEEEEEECCCCEEE	20.16	25953088
158	Malonylation	GNALCTVKCDEKVKV CCEEEEEECCCCEEE	20.16	26320211
158	Succinylation	GNALCTVKCDEKVKV CCEEEEEECCCCEEE	20.16	-
158	Succinylation	GNALCTVKCDEKVKV CCEEEEEECCCCEEE	20.16	-
158	Ubiquitination	GNALCTVKCDEKVKV CCEEEEEECCCCEEE	20.16	-
164	2-Hydroxyisobutyrylation	VKCDEKVKVFSVRGT EECCCCEEEEEEECC	48.94	-
164	Acetylation	VKCDEKVKVFSVRGT EECCCCEEEEEEECC	48.94	27452117
164	Ubiquitination	VKCDEKVKVFSVRGT EECCCCEEEEEEECC	48.94	-
167	Ubiquitination	DEKVKVFSVRGTSFD CCCEEEEEEECCEEC	17.56	21890473
169	Methylation	KVKVFSVRGTSFDAA CEEEEEEECCEECHH	41.28	-
171	Phosphorylation	KVFSVRGTSFDAAAT EEEEEECCEECHHHH	18.69	23911959
172	Phosphorylation	VFSVRGTSFDAAATS EEEEECCEECHHHHC	24.77	28258704
177	Ubiquitination	GTSFDAAATSGGSAS CCEECHHHHCCCCCC	12.20	21890473
179	Phosphorylation	SFDAAATSGGSASSE EECHHHHCCCCCCCC	36.11	21712546
182	Phosphorylation	AAATSGGSASSEKAS HHHHCCCCCCCCCCC	28.62	24275569
184	Phosphorylation	ATSGGSASSEKASST HHCCCCCCCCCCCCC	40.50	21712546
185	Phosphorylation	TSGGSASSEKASSTS HCCCCCCCCCCCCCC	42.72	21712546
187	Succinylation	GGSASSEKASSTSPV CCCCCCCCCCCCCCC	56.36	-
187	Succinylation	GGSASSEKASSTSPV CCCCCCCCCCCCCCC	56.36	-
187	Ubiquitination	GGSASSEKASSTSPV CCCCCCCCCCCCCCC	56.36	-
189	Phosphorylation	SASSEKASSTSPVEI CCCCCCCCCCCCCCH	45.26	30108239
190	Phosphorylation	ASSEKASSTSPVEIS CCCCCCCCCCCCCHH	37.45	30108239
191	Phosphorylation	SSEKASSTSPVEISE CCCCCCCCCCCCHHH	34.26	30108239
192	Phosphorylation	SEKASSTSPVEISEW CCCCCCCCCCCHHHH	28.97	30108239
197	Phosphorylation	STSPVEISEWLDQKL CCCCCCHHHHHHHHC	14.82	23186163
203	Acetylation	ISEWLDQKLTKSDRP HHHHHHHHCCCCCCC	58.76	26822725
203	Succinylation	ISEWLDQKLTKSDRP HHHHHHHHCCCCCCC	58.76	-
203	Succinylation	ISEWLDQKLTKSDRP HHHHHHHHCCCCCCC	58.76	-
203	Ubiquitination	ISEWLDQKLTKSDRP HHHHHHHHCCCCCCC	58.76	-
206	Ubiquitination	WLDQKLTKSDRPELT HHHHHCCCCCCCCCC	61.88	-
207	Phosphorylation	LDQKLTKSDRPELTG HHHHCCCCCCCCCCC	33.35	20068231
213	Phosphorylation	KSDRPELTGAKVVVS CCCCCCCCCCEEEEE	33.17	20068231
216	Malonylation	RPELTGAKVVVSGGR CCCCCCCEEEEECCC	36.59	32601280
216	Succinylation	RPELTGAKVVVSGGR CCCCCCCEEEEECCC	36.59	-
216	Succinylation	RPELTGAKVVVSGGR CCCCCCCEEEEECCC	36.59	21890473
216	Ubiquitination	RPELTGAKVVVSGGR CCCCCCCEEEEECCC	36.59	21890473
216	Ubiquitination	RPELTGAKVVVSGGR CCCCCCCEEEEECCC	36.59	21890473
223	Methylation	KVVVSGGRGLKSGEN EEEEECCCCCCCCCC	51.28	-
226	Acetylation	VSGGRGLKSGENFKL EECCCCCCCCCCHHH	60.27	23236377
226	Malonylation	VSGGRGLKSGENFKL EECCCCCCCCCCHHH	60.27	26320211
226	Succinylation	VSGGRGLKSGENFKL EECCCCCCCCCCHHH	60.27	-
226	Succinylation	VSGGRGLKSGENFKL EECCCCCCCCCCHHH	60.27	-
226	Ubiquitination	VSGGRGLKSGENFKL EECCCCCCCCCCHHH	60.27	21890473
226	Ubiquitination	VSGGRGLKSGENFKL EECCCCCCCCCCHHH	60.27	21890473
227	Phosphorylation	SGGRGLKSGENFKLL ECCCCCCCCCCHHHH	57.28	22461510
232	Acetylation	LKSGENFKLLYDLAD CCCCCCHHHHHHHHH	49.52	25038526
232	Succinylation	LKSGENFKLLYDLAD CCCCCCHHHHHHHHH	49.52	-
232	Succinylation	LKSGENFKLLYDLAD CCCCCCHHHHHHHHH	49.52	-
232	Ubiquitination	LKSGENFKLLYDLAD CCCCCCHHHHHHHHH	49.52	-
235	Phosphorylation	GENFKLLYDLADQLH CCCHHHHHHHHHHHH	21.24	20860994
248	Phosphorylation	LHAAVGASRAAVDAG HHHHHCCHHHHHHCC	19.27	20860994
261	Sulfoxidation	AGFVPNDMQVGQTGK CCCCCCCCCCCCCCC	4.40	21406390
294	2-Hydroxyisobutyrylation	LAGMKDSKTIVAINK HCCCCCCCEEEEEEC	53.02	-
294	Ubiquitination	LAGMKDSKTIVAINK HCCCCCCCEEEEEEC	53.02	-
301	Succinylation	KTIVAINKDPEAPIF CEEEEEECCCCCCCE	69.42	-
301	Succinylation	KTIVAINKDPEAPIF CEEEEEECCCCCCCE	69.42	23954790
331	Succinylation	PEMTEILKKK----- HHHHHHHHCC-----	65.27	23954790
331	Ubiquitination	PEMTEILKKK----- HHHHHHHHCC-----	65.27	-

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 ETFA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ETFA_HUMAN !!

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 ETFA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ETFB_HUMAN	ETFB	physical	22939629
NNTM_HUMAN	NNT	physical	26186194
IF2B_HUMAN	EIF2S2	physical	26186194
GLSK_HUMAN	GLS	physical	26186194
ETFB_HUMAN	ETFB	physical	26186194
ETFR1_HUMAN	LYRM5	physical	26186194
ACPM_HUMAN	NDUFAB1	physical	26186194
CH082_HUMAN	C8orf82	physical	26186194
AL1B1_HUMAN	ALDH1B1	physical	26344197
APMAP_HUMAN	APMAP	physical	26344197
ARF4_HUMAN	ARF4	physical	26344197
ARF5_HUMAN	ARF5	physical	26344197
ARL8B_HUMAN	ARL8B	physical	26344197
ATPA_HUMAN	ATP5A1	physical	26344197
ATPG_HUMAN	ATP5C1	physical	26344197
BCAT2_HUMAN	BCAT2	physical	26344197
TCPG_HUMAN	CCT3	physical	26344197
KCY_HUMAN	CMPK1	physical	26344197
GPX4_HUMAN	GPX4	physical	26344197
HERC2_HUMAN	HERC2	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
NIT1_HUMAN	NIT1	physical	26344197
PO210_HUMAN	NUP210	physical	26344197
PEF1_HUMAN	PEF1	physical	26344197
RAB2A_HUMAN	RAB2A	physical	26344197
RAB6A_HUMAN	RAB6A	physical	26344197
RAB6B_HUMAN	RAB6B	physical	26344197
RDH13_HUMAN	RDH13	physical	26344197
SUCB1_HUMAN	SUCLA2	physical	26344197
SUCB2_HUMAN	SUCLG2	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
ETFB_HUMAN	ETFB	physical	28514442
CH082_HUMAN	C8orf82	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
231680	Glutaric aciduria 2A (GA2A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ETFA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42, AND MASSSPECTROMETRY.	17081983 [Abstract]