SDHA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SDHA_MOUSE
• UniProt AC: Q8K2B3
• Protein Name: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
• Gene Name: Sdha
• Organism: Mus musculus (Mouse).
• Sequence Length: 664
• Subcellular Localization: Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side .
• Protein Description: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor..
• Protein Sequence: MAGVGAVSRLLRGRRLALTGAWPGTLQKQTCGFHFSVGENKKASAKVSDAISTQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACLTKLFPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSDWLGDQDAIHYMTEQAPASVVELENYGMPFSRTEDGKIYQRAFGGQSLKFGKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIEDGSIHRIRAKNTVIATGGYGRTYFSCTSAHTSTGDGTAMVTRAGLPCQDLEFVQFHPTGIYGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPEKDHVYLQLHHLPPEQLATRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQVLKHVNGQDQIVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIAESCRPGDKVPSIKANAGEESVMNLDKLRFADGSIRTSELRLNMQKSMQNHAAVFRVGSVLQEGCEKISQLYGDLKHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDYKVRVDEYDYSKPIQGQQKKPFGEHWRKHTLSYVDIKTGKVTLEYRPVIDKTLNEADCATVPPAIRSY

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
8	Phosphorylation	MAGVGAVSRLLRGRR CCCHHHHHHHHHCCC		-
89	S-nitrosocysteine	EAGFNTACLTKLFPT CCCCCHHHHHHHCCC		-
89	S-palmitoylation	EAGFNTACLTKLFPT CCCCCHHHHHHHCCC		28526873
92	Acetylation	FNTACLTKLFPTRSH CCHHHHHHHCCCCCH		24062335
96	Phosphorylation	CLTKLFPTRSHTVAA HHHHHCCCCCHHHHH		23140645
98	Phosphorylation	TKLFPTRSHTVAAQG HHHCCCCCHHHHHCC		23140645
99	Tele-8alpha-FAD histidine	KLFPTRSHTVAAQGG HHCCCCCHHHHHCCC		-
99	Other	KLFPTRSHTVAAQGG HHCCCCCHHHHHCCC		-
100	Phosphorylation	LFPTRSHTVAAQGGI HCCCCCHHHHHCCCH		21082442
128	Acetylation	WHFYDTVKGSDWLGD EEEEECCCCCCCCCC		23864654
167	Acetylation	FSRTEDGKIYQRAFG CCCCCCCCEEEEECC		23576753
167	Succinylation	FSRTEDGKIYQRAFG CCCCCCCCEEEEECC		23806337
169	Phosphorylation	RTEDGKIYQRAFGGQ CCCCCCEEEEECCCC		22802335
179	Acetylation	AFGGQSLKFGKGGQA ECCCCCCEECCCCCC		21858060
179	Glutarylation	AFGGQSLKFGKGGQA ECCCCCCEECCCCCC		24703693
179	Malonylation	AFGGQSLKFGKGGQA ECCCCCCEECCCCCC		26073543
179	Succinylation	AFGGQSLKFGKGGQA ECCCCCCEECCCCCC		-
179	Succinylation	AFGGQSLKFGKGGQA ECCCCCCEECCCCCC		23806337
179	Ubiquitination	AFGGQSLKFGKGGQA ECCCCCCEECCCCCC		-
182	Acetylation	GQSLKFGKGGQAHRC CCCCEECCCCCCEEE		21858060
182	Glutarylation	GQSLKFGKGGQAHRC CCCCEECCCCCCEEE		24703693
215	Phosphorylation	SLRYDTSYFVEYFAL CCCCCCHHHHHHHHH		-
238	S-nitrosocysteine	CRGVIALCIEDGSIH CCEEEEEEECCCCEE		-
238	S-palmitoylation	CRGVIALCIEDGSIH CCEEEEEEECCCCEE		28526873
250	Acetylation	SIHRIRAKNTVIATG CEEEEEECCEEEEEC		21858060
250	Glutarylation	SIHRIRAKNTVIATG CEEEEEECCEEEEEC		24703693
250	Succinylation	SIHRIRAKNTVIATG CEEEEEECCEEEEEC		-
250	Succinylation	SIHRIRAKNTVIATG CEEEEEECCEEEEEC		23806337
252	Phosphorylation	HRIRAKNTVIATGGY EEEEECCEEEEECCC		-
266	S-nitrosocysteine	YGRTYFSCTSAHTST CCCEEEEEEECEECC		-
266	S-palmitoylation	YGRTYFSCTSAHTST CCCEEEEEEECEECC		28526873
287	S-palmitoylation	VTRAGLPCQDLEFVQ EECCCCCCCCCEEEE		28526873
305	S-palmitoylation	TGIYGAGCLITEGCR CCEECCCEEEECCCC		28526873
311	S-palmitoylation	GCLITEGCRGEGGIL CEEEECCCCCCCCEE		28526873
335	Acetylation	ERYAPVAKDLASRDV HHHHHHHHHHHCCCC		21858060
335	Glutarylation	ERYAPVAKDLASRDV HHHHHHHHHHHCCCC		24703693
335	Succinylation	ERYAPVAKDLASRDV HHHHHHHHHHHCCCC		-
335	Succinylation	ERYAPVAKDLASRDV HHHHHHHHHHHCCCC		23806337
335	Ubiquitination	ERYAPVAKDLASRDV HHHHHHHHHHHCCCC		27667366
357	S-nitrosocysteine	EIREGRGCGPEKDHV EEECCCCCCCCCCCE		-
361	Acetylation	GRGCGPEKDHVYLQL CCCCCCCCCCEEEEE		23864654
365	Phosphorylation	GPEKDHVYLQLHHLP CCCCCCEEEEECCCC		25195567
423	Acetylation	NYKGQVLKHVNGQDQ CCCCCEEEECCCCCC		23576753
423	Methylation	NYKGQVLKHVNGQDQ CCCCCEEEECCCCCC		-
438	S-palmitoylation	IVPGLYACGEAACAS CCCCEEHHHHHHHHH		28680068
456	Phosphorylation	ANRLGANSLLDLVVF CCCCCCCHHHHHHHH		-
467	S-palmitoylation	LVVFGRACALSIAES HHHHHHHHHHHHHHH		28526873
475	S-palmitoylation	ALSIAESCRPGDKVP HHHHHHHCCCCCCCC		28526873
480	Acetylation	ESCRPGDKVPSIKAN HHCCCCCCCCCCCCC		21858060
480	Glutarylation	ESCRPGDKVPSIKAN HHCCCCCCCCCCCCC		24703693
480	Malonylation	ESCRPGDKVPSIKAN HHCCCCCCCCCCCCC		26320211
480	Succinylation	ESCRPGDKVPSIKAN HHCCCCCCCCCCCCC		24315375
483	Phosphorylation	RPGDKVPSIKANAGE CCCCCCCCCCCCCCC		23140645
485	Acetylation	GDKVPSIKANAGEES CCCCCCCCCCCCCCC		21858060
485	Glutarylation	GDKVPSIKANAGEES CCCCCCCCCCCCCCC		24703693
485	Succinylation	GDKVPSIKANAGEES CCCCCCCCCCCCCCC		-
485	Succinylation	GDKVPSIKANAGEES CCCCCCCCCCCCCCC		23806337
498	Acetylation	ESVMNLDKLRFADGS CCCCCHHHCEECCCC		21858060
498	Glutarylation	ESVMNLDKLRFADGS CCCCCHHHCEECCCC		24703693
498	Succinylation	ESVMNLDKLRFADGS CCCCCHHHCEECCCC		-
498	Succinylation	ESVMNLDKLRFADGS CCCCCHHHCEECCCC		23806337
498	Ubiquitination	ESVMNLDKLRFADGS CCCCCHHHCEECCCC		-
505	Phosphorylation	KLRFADGSIRTSELR HCEECCCCCCHHHHH		23737553
508	Phosphorylation	FADGSIRTSELRLNM ECCCCCCHHHHHHHH		23737553
509	Phosphorylation	ADGSIRTSELRLNMQ CCCCCCHHHHHHHHH		23737553
517	Acetylation	ELRLNMQKSMQNHAA HHHHHHHHHHHHCHH		23576753
517	Malonylation	ELRLNMQKSMQNHAA HHHHHHHHHHHHCHH		26320211
517	Ubiquitination	ELRLNMQKSMQNHAA HHHHHHHHHHHHCHH		-
530	Phosphorylation	AAVFRVGSVLQEGCE HHHHHHHHHHHHHHH		25521595
536	S-nitrosocysteine	GSVLQEGCEKISQLY HHHHHHHHHHHHHHH		-
536	S-palmitoylation	GSVLQEGCEKISQLY HHHHHHHHHHHHHHH		28526873
538	Acetylation	VLQEGCEKISQLYGD HHHHHHHHHHHHHHH		23576753
538	Succinylation	VLQEGCEKISQLYGD HHHHHHHHHHHHHHH		-
538	Succinylation	VLQEGCEKISQLYGD HHHHHHHHHHHHHHH		23806337
543	Phosphorylation	CEKISQLYGDLKHLK HHHHHHHHHHHHHCC		-
547	Acetylation	SQLYGDLKHLKTFDR HHHHHHHHHCCCCCC		21858060
547	Glutarylation	SQLYGDLKHLKTFDR HHHHHHHHHCCCCCC		24703693
547	Succinylation	SQLYGDLKHLKTFDR HHHHHHHHHCCCCCC		-
547	Succinylation	SQLYGDLKHLKTFDR HHHHHHHHHCCCCCC		23806337
547	Ubiquitination	SQLYGDLKHLKTFDR HHHHHHHHHCCCCCC		-
550	Acetylation	YGDLKHLKTFDRGMV HHHHHHCCCCCCCCC		21858060
550	Glutarylation	YGDLKHLKTFDRGMV HHHHHHCCCCCCCCC		24703693
550	Succinylation	YGDLKHLKTFDRGMV HHHHHHCCCCCCCCC		23954790
598	Acetylation	AHAREDYKVRVDEYD CCCCCCCEEEECCCC		21858060
598	Succinylation	AHAREDYKVRVDEYD CCCCCCCEEEECCCC		24315375
604	Phosphorylation	YKVRVDEYDYSKPIQ CEEEECCCCCCCCCC		25195567
608	Acetylation	VDEYDYSKPIQGQQK ECCCCCCCCCCCCCC		21858060
608	Glutarylation	VDEYDYSKPIQGQQK ECCCCCCCCCCCCCC		24703693
608	Malonylation	VDEYDYSKPIQGQQK ECCCCCCCCCCCCCC		26320211
608	Succinylation	VDEYDYSKPIQGQQK ECCCCCCCCCCCCCC		24315375
615	Acetylation	KPIQGQQKKPFGEHW CCCCCCCCCCCCHHH		23806337
615	Glutarylation	KPIQGQQKKPFGEHW CCCCCCCCCCCCHHH		24703693
615	Succinylation	KPIQGQQKKPFGEHW CCCCCCCCCCCCHHH		-
615	Succinylation	KPIQGQQKKPFGEHW CCCCCCCCCCCCHHH		23806337
616	Acetylation	PIQGQQKKPFGEHWR CCCCCCCCCCCHHHH		24062335
616	Glutarylation	PIQGQQKKPFGEHWR CCCCCCCCCCCHHHH		24703693
624	Acetylation	PFGEHWRKHTLSYVD CCCHHHHHCEEEEEE		21858060
629	Phosphorylation	WRKHTLSYVDIKTGK HHHCEEEEEEECCCE		22817900
633	Acetylation	TLSYVDIKTGKVTLE EEEEEEECCCEEEEE		21858060
633	Succinylation	TLSYVDIKTGKVTLE EEEEEEECCCEEEEE		24315375
633	Ubiquitination	TLSYVDIKTGKVTLE EEEEEEECCCEEEEE		-
636	Acetylation	YVDIKTGKVTLEYRP EEEECCCEEEEEEEE		23576753
636	Glutarylation	YVDIKTGKVTLEYRP EEEECCCEEEEEEEE		24703693
636	Succinylation	YVDIKTGKVTLEYRP EEEECCCEEEEEEEE		23806337
638	Phosphorylation	DIKTGKVTLEYRPVI EECCCEEEEEEEECC		22817900
641	Phosphorylation	TGKVTLEYRPVIDKT CCEEEEEEEECCCCC		22817900
647	Acetylation	EYRPVIDKTLNEADC EEEECCCCCCCHHHH		23576753
654	S-nitrosocysteine	KTLNEADCATVPPAI CCCCHHHHCCCCHHH		-
654	S-palmitoylation	KTLNEADCATVPPAI CCCCHHHHCCCCHHH		28526873
663	Phosphorylation	TVPPAIRSY------ CCCHHHHCC------		30165576
664	Phosphorylation	VPPAIRSY------- CCHHHHCC-------		30165576

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
215	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
604	Y	Phosphorylation	Kinase	FGR	P14234	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
498	K	Acetylation	Acetylation of Lys-498 and Lys-538 is observed in liver mitochondria from fasted mice but not from fed mice.	21858060
538	K	Acetylation	Acetylation of Lys-498 and Lys-538 is observed in liver mitochondria from fasted mice but not from fed mice.	23806337

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of SDHA_MOUSE !!

Drug and Disease Associations

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