UniProt Accession

 DHSA_MOUSE; Q8K2B3; Q0QF19; Q3UH25; Q3UKP7; Q3V4B1; Q921P5; Q9Z1Z4 

Genbank Protein ID

 AK029520; AK034928; AK049590; AK050475; AK075990; AK145923; AK147286; AK147624; AK153085; AK162148; AK169254; AK004362; BC011301; BC031849; DQ402975; AF095938 

Genbank Nucleotide ID

 BAC26491.1; BAC28884.1; BAC33831.1; BAC34276.1; BAC36101.1; BAE26754.1; BAE27822.1; BAE28032.1; BAE31710.1; BAE36754.1; BAE41018.1; BAE43173.1; AAH11301.1; AAH31849.1; ABD77308.1; AAC72373.1 

Protein Name

 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial 

Protein Synonyms/Alias

 Flavoprotein subunit of complex II; Fp 

Gene Name

 Sdha 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
128	WHFYDTVKGSDWLGD	acetylation	[1]
167	FSRTEDGKIYQRAFG	acetylation	[1, 2, 3, 4]
167	FSRTEDGKIYQRAFG	succinylation	[4]
179	AFGGQSLKFGKGGQA	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 9]
179	AFGGQSLKFGKGGQA	succinylation	[4]
179	AFGGQSLKFGKGGQA	ubiquitination	[10]
182	GQSLKFGKGGQAHRC	acetylation	[1, 2, 3, 7]
250	SIHRIRAKNTVIATG	acetylation	[4]
250	SIHRIRAKNTVIATG	succinylation	[4]
335	ERYAPVAKDLASRDV	acetylation	[1, 2, 3, 4, 7, 8]
335	ERYAPVAKDLASRDV	succinylation	[4]
335	ERYAPVAKDLASRDV	ubiquitination	[10]
361	GRGCGPEKDHVYLQL	acetylation	[1, 2]
423	NYKGQVLKHVNGQDQ	acetylation	[1, 2, 3, 5]
480	ESCRPGDKVPSIKAN	acetylation	[1, 2, 3, 8]
485	GDKVPSIKANAGEES	acetylation	[4, 5]
485	GDKVPSIKANAGEES	succinylation	[4]
498	ESVMNLDKLRFADGS	acetylation	[1, 2, 3, 4, 5, 7, 11]
498	ESVMNLDKLRFADGS	succinylation	[4]
498	ESVMNLDKLRFADGS	ubiquitination	[10]
517	ELRLNMQKSMQNHAA	acetylation	[1, 2, 3, 8]
517	ELRLNMQKSMQNHAA	ubiquitination	[10]
538	VLQEGCEKISQLYGD	acetylation	[1, 2, 3, 4, 5, 7, 11]
538	VLQEGCEKISQLYGD	succinylation	[4]
547	SQLYGDLKHLKTFDR	acetylation	[1, 2, 3, 4, 5, 6, 7, 8, 11]
547	SQLYGDLKHLKTFDR	succinylation	[4]
547	SQLYGDLKHLKTFDR	ubiquitination	[10]
550	YGDLKHLKTFDRGMV	acetylation	[1, 2, 8]
598	AHAREDYKVRVDEYD	acetylation	[1, 2, 3]
608	VDEYDYSKPIQGQQK	acetylation	[1, 2, 3, 4, 6, 7, 8, 9, 11]
615	KPIQGQQKKPFGEHW	acetylation	[1, 4]
615	KPIQGQQKKPFGEHW	succinylation	[4]
616	PIQGQQKKPFGEHWR	acetylation	[8]
624	PFGEHWRKHTLSYVD	acetylation	[8]
633	TLSYVDIKTGKVTLE	acetylation	[1, 2, 3]
633	TLSYVDIKTGKVTLE	ubiquitination	[10]
636	YVDIKTGKVTLEYRP	acetylation	[2, 3, 4]
636	YVDIKTGKVTLEYRP	succinylation	[4]
647	EYRPVIDKTLNEADC	acetylation	[1, 2, 3]

Reference

 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [6] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [8] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [11] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599] 

Functional 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) (By similarity). Can act as a tumor suppressor (By similarity). 

Sequence Annotation

 NP_BIND 68 73 FAD (By similarity).
 NP_BIND 91 106 FAD (By similarity).
 NP_BIND 456 457 FAD (By similarity).
 ACT_SITE 340 340 Proton acceptor (By similarity).
 BINDING 275 275 FAD (By similarity).
 BINDING 296 296 Substrate (By similarity).
 BINDING 308 308 Substrate (By similarity).
 BINDING 407 407 Substrate (By similarity).
 BINDING 440 440 FAD (By similarity).
 BINDING 451 451 Substrate (By similarity).
 MOD_RES 99 99 Tele-8alpha-FAD histidine (By
 MOD_RES 179 179 N6-acetyllysine.
 MOD_RES 215 215 Phosphotyrosine; by SRC (By similarity).
 MOD_RES 252 252 Phosphothreonine.
 MOD_RES 335 335 N6-acetyllysine (By similarity).
 MOD_RES 423 423 N6-acetyllysine.
 MOD_RES 485 485 N6-acetyllysine.
 MOD_RES 498 498 N6-acetyllysine.
 MOD_RES 538 538 N6-acetyllysine.
 MOD_RES 547 547 N6-acetyllysine.
 MOD_RES 608 608 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle; Tumor suppressor. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 664 AA 

Protein Sequence

Gene Ontology

 GO:0005749; C:mitochondrial respiratory chain complex II; ISS:UniProtKB.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:EC.
 GO:0007399; P:nervous system development; IEA:Compara.
 GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
 GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 

Interpro

 IPR003953; FAD_bind_dom.
 IPR003952; FRD_SDH_FAD_BS.
 IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
 IPR027477; Succ_DH/fumarate_Rdtase_cat.
 IPR011281; Succ_DH_flav_su_fwd.
 IPR014006; Succ_Dhase_FrdA_Gneg. 

Pfam

 PF00890; FAD_binding_2
 PF02910; Succ_DH_flav_C 

SMART

  

PROSITE

 PS00504; FRD_SDH_FAD_BINDING 

PRINTS