CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018454
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial 
Protein Synonyms/Alias
 Complex I-75kD; CI-75kD 
Gene Name
 Ndufs1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
84MCLVEIEKAPKVVAAacetylation[1, 2, 3, 4, 5, 6, 7, 8]
84MCLVEIEKAPKVVAAsuccinylation[7]
98ACAMPVMKGWNILTNacetylation[8]
108NILTNSEKSKKAREGacetylation[4, 8]
170KNIGPLVKTIMTRCIubiquitination[9]
298RFAYDGLKRQRLTEPubiquitination[9]
311EPMVRNEKGLLTYTSacetylation[2, 4, 8]
311EPMVRNEKGLLTYTSubiquitination[9]
450DHLGDSPKILQDIASacetylation[4, 6, 7, 8]
450DHLGDSPKILQDIASsuccinylation[7]
467HSFCEVLKDAKKPMVacetylation[2, 4, 5, 6, 8]
470CEVLKDAKKPMVVLGacetylation[4]
499AVSNMVQKIRVTTGVacetylation[6, 8]
531AALDLGYKPGVEAIRubiquitination[9]
543AIRKNPPKMLFLLGAacetylation[4, 8]
562ITRQDLPKDCFIVYQacetylation[4, 8]
709RASQTMAKCVKAVTEacetylation[4, 6, 7, 8]
709RASQTMAKCVKAVTEsuccinylation[7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
 Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized (By similarity). 
Sequence Annotation
 DOMAIN 30 108 2Fe-2S ferredoxin-type.
 DOMAIN 245 301 4Fe-4S Mo/W bis-MGD-type.
 METAL 64 64 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 75 75 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 78 78 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 92 92 Iron-sulfur 1 (2Fe-2S) (By similarity).
 METAL 124 124 Iron-sulfur 2 (4Fe-4S); via pros nitrogen
 METAL 128 128 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 131 131 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 137 137 Iron-sulfur 2 (4Fe-4S) (By similarity).
 METAL 176 176 Iron-sulfur 3 (4Fe-4S) (By similarity).
 METAL 179 179 Iron-sulfur 3 (4Fe-4S) (By similarity).
 METAL 182 182 Iron-sulfur 3 (4Fe-4S) (By similarity).
 METAL 226 226 Iron-sulfur 3 (4Fe-4S) (By similarity).
 MOD_RES 84 84 N6-acetyllysine.  
Keyword
 2Fe-2S; 4Fe-4S; Acetylation; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide; Transport; Ubiquinone. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 727 AA 
Protein Sequence
MLRIPIKRAL IGLSNSPKGY VRTTGTAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 60
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 120
LANHPLDCPI CDQGGECDLQ DQSMMFGSDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 180
RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NVIDICPVGA LTSKPYAFTA 240
RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 300
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QNFEGNAVAA IAGGLVDAEA LVALKDLLNK 360
VDSDNLCTEE IFPTEGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 420
SWLHNDLKVA LIGSPVDLTY RYDHLGDSPK ILQDIASGRH SFCEVLKDAK KPMVVLGSSA 480
LQRDDGAAIL VAVSNMVQKI RVTTGVAAEW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 540
PPKMLFLLGA DGGCITRQDL PKDCFIVYQG HHGDVGAPMA DVILPGAAYT EKSATYVNTE 600
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GITLPYDTLD QVRNRLEEVS PNLVRYDDIE 660
ETNYFQQASE LAKLVNQEVL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA 720
VEEPSIC 727 
Gene Ontology
 GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
 GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:RefGenome.
 GO:0008637; P:apoptotic mitochondrial changes; ISS:UniProtKB.
 GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
 GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
 GO:0045333; P:cellular respiration; ISS:UniProtKB.
 GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
 GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB. 
Interpro
 IPR001041; 2Fe-2S_ferredoxin-type.
 IPR012675; Beta-grasp_dom.
 IPR006656; Mopterin_OxRdtase.
 IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
 IPR010228; NADH_UbQ_OxRdtase_Gsu.
 IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
 IPR015405; NuoG_C. 
Pfam
 PF09326; DUF1982
 PF00384; Molybdopterin
 PF10588; NADH-G_4Fe-4S_3 
SMART
 SM00929; NADH-G_4Fe-4S_3 
PROSITE
 PS00197; 2FE2S_FER_1
 PS51085; 2FE2S_FER_2
 PS51669; 4FE4S_MOW_BIS_MGD
 PS00641; COMPLEX1_75K_1
 PS00642; COMPLEX1_75K_2
 PS00643; COMPLEX1_75K_3 
PRINTS