CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020510
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial 
Protein Synonyms/Alias
 Iron-sulfur subunit of complex II; Ip 
Gene Name
 Sdhb 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
43AAAPRIKKFAIYRWDacetylation[1, 2, 3]
53IYRWDPDKTGDKPRMacetylation[3, 4, 5]
57DPDKTGDKPRMQTYEacetylation[3, 4, 5]
69TYEVDLNKCGPMVLDacetylation[6]
125RIDTDLSKVSKIYPLacetylation[4]
128TDLSKVSKIYPLPHMacetylation[4, 6]
139LPHMYVIKDLVPDLSacetylation[5]
160KSIEPYLKKKDESQEacetylation[3, 4, 5]
169KDESQEGKQQYLQSIacetylation[3, 5]
235FTEERLAKLQDPFSVacetylation[2, 3]
235FTEERLAKLQDPFSVubiquitination[7]
269GKAIAEIKKMMATYKacetylation[3, 4]
276KKMMATYKEKRALA*acetylation[4, 8]
276KKMMATYKEKRALA*succinylation[8]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Iron-sulfur protein (IP) 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). 
Sequence Annotation
 DOMAIN 42 135 2Fe-2S ferredoxin-type.
 DOMAIN 178 208 4Fe-4S ferredoxin-type.
 METAL 95 95 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 100 100 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 103 103 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 115 115 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 188 188 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 191 191 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 194 194 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 198 198 Iron-sulfur 3 (3Fe-4S) (By similarity).
 METAL 245 245 Iron-sulfur 3 (3Fe-4S) (By similarity).
 METAL 251 251 Iron-sulfur 3 (3Fe-4S) (By similarity).
 METAL 255 255 Iron-sulfur 2 (4Fe-4S) (By similarity).
 BINDING 203 203 Ubiquinone; shared with DHSD (By  
Keyword
 2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 282 AA 
Protein Sequence
MAATVGVSLK RGFPAAVLGR VGLQFQACRG AQTAAAAAPR IKKFAIYRWD PDKTGDKPRM 60
QTYEVDLNKC GPMVLDALIK IKNEVDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID 120
TDLSKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE 180
KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDDFTE ERLAKLQDPF 240
SVYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA 282 
Gene Ontology
 GO:0005749; C:mitochondrial respiratory chain complex II; ISS:UniProtKB.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
 GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:EC.
 GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
 GO:0022904; P:respiratory electron transport chain; IEA:Compara.
 GO:0006105; P:succinate metabolic process; IEA:Compara.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 
Interpro
 IPR001041; 2Fe-2S_ferredoxin-type.
 IPR006058; 2Fe2S_fd_BS.
 IPR017896; 4Fe4S_Fe-S-bd.
 IPR017900; 4Fe4S_Fe_S_CS.
 IPR012675; Beta-grasp_dom.
 IPR012285; Fum_reductase_C.
 IPR009051; Helical_ferredxn.
 IPR004489; Succ_DH/fum_Rdtase_Fe-S.
 IPR025192; Succ_DH/fum_Rdtase_N. 
Pfam
 PF13085; Fer2_3 
SMART
  
PROSITE
 PS00197; 2FE2S_FER_1
 PS51085; 2FE2S_FER_2
 PS00198; 4FE4S_FER_1
 PS51379; 4FE4S_FER_2 
PRINTS