CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036267
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 SDHA 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41HFTVDGNKRASAKVSubiquitination[1]
92FNTACVTKLFPTRSHubiquitination[2, 3]
167FSRTEDGKIYQRAFGubiquitination[1, 4]
179AFGGQSLKFGKGGQAacetylation[5, 6]
179AFGGQSLKFGKGGQAubiquitination[1, 2, 4, 6, 7, 8]
250SIHRIRAKNTVVATGubiquitination[1, 7]
335ERYAPVAKDLASRDVubiquitination[1, 2, 4, 6]
527IDEYDYSKPIQGQQKacetylation[5, 9]
527IDEYDYSKPIQGQQKubiquitination[1, 2, 3, 7]
535PIQGQQKKPFEEHWRubiquitination[4]
543PFEEHWRKHTLSYVDubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 583 AA 
Protein Sequence
MSGVRGLSRL LSARRLALAK AWPTVLQTGT RGFHFTVDGN KRASAKVSDS ISAQYPVVDH 60
EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR 120
WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF 180
GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE 240
DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI 300
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE 360
KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ 420
VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IEESCRPGDK 480
VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKVRI DEYDYSKPIQ GQQKKPFEEH 540
WRKHTLSYVD VGTGKVTLEY RPVIDKTLNE ADCATVPPAI RSY 583 
Gene Ontology
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
 GO:0022900; P:electron transport chain; IEA:InterPro.
 GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 
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